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Epilepsie

L’épilepsie, aussi appelée mal comitial, est une affection neurologique définie depuis 2005 par la ligue internationale contre l’épilepsie (ILAE) par une prédisposition cérébrale à générer des crises épileptiques dites « non provoquées », c’est-à-dire non expliquées par un facteur causal immédiat. Une crise épileptique est caractérisée par une altération fonctionnelle transitoire au sein d’une population de neurones (soit limitée à une région du cerveau : crise dite « partielle », soit impliquant les deux hémisphères cérébraux de manière simultanée : crise dite « généralisée ») due à une décharge épileptique.

Un facteur prédisposant peut être d’origine génétique, lésionnel (lésion cérébrale présente depuis la naissance, malformative, ou acquise au cours de la vie, comme un accident vasculaire cérébral ou les complications d’un traumatisme crânien grave), ou autre (par exemple, une anomalie de l’électro-encéphalogramme peut être considérée comme prédisposant).

Il n’existe pas une seule épilepsie, mais de nombreuses formes différentes, à l’origine de crises épileptiques elles-mêmes très variées (crise tonico-clonique généralisée ou convulsions, crise myoclonique, absence épileptique, crise partielle simple, crise partielle complexe, sont les plus fréquentes). Une épilepsie est caractérisée par deux traits essentiels : le caractère « généralisé » (les crises intéressent d’emblée les deux hémisphères cérébraux) ou « partiel » (les crises n’intéressent qu’une population limitée de neurones), et leur étiologie (« idiopathique » ou « génétique », et « symptomatique » ou « structurel/métabolique », selon les anciennes et nouvelles terminologies, respectivement).

Chez les personnes souffrant d’épilepsie, la survenue d’une crise est souvent due à un état de fatigue inhabituel, un manque de sommeil, ou un état anxieux. Dans une minorité de cas dits « photosensibles », une stimulation lumineuse intermittente (par exemple, un stroboscope) peut être à l’origine des crises.

Causes

Il existe une classification internationale des épilepsies (en). Les causes de l’épilepsie sont très nombreuses, tout le monde peut être concerné par l’apparition d’une crise d’épilepsie sans pour autant « être épileptique ». Un certain nombre d’affections diminuent la résistance à lutter contre la propagation de la décharge électrique dans le cerveau. Une baisse du seuil épileptogène serait responsable de la crise d’épilepsie.

Des crises occasionnelles, survenant dans des conditions particulières, peuvent être causées notamment par convulsions fébriles, hypoglycémie, troubles ioniques, hypocalcémie, hyponatrémie, alcoolisme, ivresse aiguë, sevrage alcoolique, surdosage en médicaments (théophylline) ou sevrage en médicament antiépileptique (benzodiazépines).

Les épilepsies symptomatiques peuvent être causées par tumeur cérébrale, accident vasculaire cérébral, encéphalite, traumatisme crânien et la maladie d’Alzheimer (il s’agit d’une complication méconnue, mais à la fois non systématique et à un stade avancé de cette pathologie4). Dans le cas du traumatisme crânien, une contusion cérébrale avec perte de connaissance après traumatisme, sans lésion cérébrale démontrée, double le risque de survenue d’une épilepsie. Ce risque reste majoré plus de 10 ans après l’accident initial.

D’autres types d’épilepsies incluent l’épilepsie cryptogénique (voir les syndromes épileptiques ci-dessus) dont une cause organique supposée existe, mais qui ne peut être mise en évidence, l’épilepsie idiopathique (aucune cause décelée ni suspectée), la chorée de Huntington (qui se présente surtout chez des cas jeunes) et l’épilepsie dans le contexte du syndrome du chromosome 20 en anneau.

Il existe des formes familiales d’épilepsie faisant suspecter une cause génétique, mais dont l’étude n’est pas aisée : une crise convulsive chez un individu peut survenir pour de multiples raisons, et toutes les convulsions ne sont pas dues à une maladie épileptique mais au franchissement du seuil épileptogène ; les maladies épileptiques n’étant que des affections ayant pour corollaire la baisse de ce seuil à un niveau anormalement bas. Ce seuil est facilement franchissable lors de petites provocations rencontrées dans la vie quotidienne (jeûne, alcool, fatigue, drogues fortes…).

Il semble que les maladies auto-immunes soient un facteur prédisposant à l’épilepsie.

Il semble que l’exposition prénatale à l’alcool augmente le risque d’épilepsie.

La convulsion fébrile en pédiatrie peut également mener au développement de l’épilepsie, mais cette cause est plutôt rare. En effet, environ 1 enfant sur 40 va développer de l’épilepsie suite aux épisodes de convulsions fébriles en pédiatrie.

Diagnostic – Signes et symptômes

L’épilepsie est un symptôme neurologique causé par un dysfonctionnement passager du cerveau ; certains disent qu’il « court-circuite ». Lors d’une crise d’épilepsie, les neurones (cellules nerveuses cérébrales) produisent soudainement une décharge électrique anormale dans certaines zones cérébrales.

Bien que l’épilepsie touche un grand nombre de personnes par ailleurs normales, le prévalence de ce trouble est fréquente chez les personnes atteintes d’arriération mentale. Réciproquement, 30% des enfants atteints d’épilepsie ont également un retard de développement. Chez l’enfant, une blessure au cerveau après la naissance est associé à une forte prévalence de l’épilepsie (75%).

Tout le monde peut être concerné par une première crise d’épilepsie, mais dans la moitié des cas il n’y en aura plus jamais d’autres. Il n’était jusque-là question d’épilepsie que si les crises se répétaient, mais depuis 2006 les médecins s’accordent à dire qu’une seule suffit pour être épileptique.

Chez l’enfant

Chez les enfants, l’épilepsie disparaît à l’adolescence dans six cas sur 10, lorsque les circuits neuronaux ont fini leur développement. Dans deux autres cas sur 10, les médicaments peuvent être supprimés après plusieurs années de traitement sans crise.

Le valium et le phénobarbital stoppent dans un premier temps les crises épileptiques de l’enfant, mais peuvent les aggraver après plusieurs traitements. Ces médicaments renforcent en effet l’action du GABA10, médiateur de l’inhibition cérébrale, qui permet en temps normal l’entrée d’ions chlorure (négatifs) dans le neurone, en se fixant sur son récepteur GABAR (molécule–canal). Or, il est montré chez le rat de laboratoire que le GABA – après plusieurs crises – est responsable d’un excès d’accumulation d’ions chlorure dans les neurones11. Le GABA cause alors une sortie excessive d’ions chlorure (sortie renforcée par le phénobarbital). De plus, au fur et à mesure des crises, le transporteur KCC2 – expulsant des ions chlorure – fonctionne moins bien, alors que NKCC1 – un autre cotransporteur expulsant des ions chlorure – continue à fonctionner12. Un diurétique précocement prescrit avec le phénobarbital, en freinant l’activité de KNCC1 du rein, permettrait de diminuer le risque de crise.

Crises généralisées

La crise tonico-clonique, ou « grand mal », représente la forme la plus spectaculaire de crise d’épilepsie. Le patient perd connaissance brutalement et son organisme présente des manifestations évoluant en trois phases : phase tonique, causant raidissement, contraction de l’ensemble des muscles des membres, du tronc et du visage dont les muscles oculomoteurs et masticateurs ; phase clonique causant des convulsions, contractions désordonnées des mêmes muscles et récupération, phase stertoreuse (perte de connaissance se prolongeant durant quelques minutes à quelques heures), caractérisée par une respiration bruyante due à l’encombrement bronchique. Cette phase est une phase de relaxation intense durant laquelle il est possible mais pas systématique de perdre ses urines. Le retour à la conscience est progressif, il existe souvent une confusion post-critique et l’absence de souvenir de la crise.

Les absences représentent une forme fréquente d’épilepsie et concernent quasiment exclusivement les enfants (jusqu’à la puberté). Elles se manifestent par une perte brusque du contact avec regard vitreux, aréactivité aux stimuli, des phénomènes cloniques (clignement des paupières, spasmes de la face, mâchonnements), parfois toniques (raidissement du tronc) ou végétatifs (perte d’urines, hypersalivation). Dans les absences typiques, la perte de conscience et le retour à la conscience sont brutaux, l’absence durant quelques secondes. Les chutes au sol sont rares. Dans certains cas, l’absence n’est ni précédée de symptômes précurseurs, ni suivie d’un ressenti particulier. Aussi, sans témoignage extérieur, la personne épileptique n’a parfois aucun moyen de savoir qu’elle a fait une crise. Elles sont contemporaines d’une activité EEG caractéristique : pointes-ondes de 3Hz, bilatérales, symétriques et synchrones.
Les absences peuvent se répéter dix à cent fois par jour en l’absence de traitement.

Les myoclonies, également une cause, se manifestent par des secousses musculaires brutales, rythmées, intenses, bilatérales ou unilatérales et synchrones, concernant les bras ou les jambes, sans perte de la conscience mais occasionnant des chutes au sol.

Le diagnostic n’est cependant pas toujours évident. Ainsi une syncope d’origine cardiaque peut se manifester, outre la perte de connaissance, par des mouvements cloniques. Le moniteur cardiaque implantable peut ainsi redresser un certain nombre de diagnostic erroné d’épilepsie qui sont « guéris » par la pose d’un stimulateur cardiaque.

Crises partielles

La symptomatologie est extrêmement polymorphe (il peut y avoir de nombreux symptômes) : le foyer épileptique est circonscrit à une zone limitée du cerveau, et entraîne des signes cliniques corrélés à la zone touchée. Les signes peuvent être l’un des items suivant :

  • des hallucinations sensorielles (visuelles, auditives, gustatives, vertigineuses)
  • des mouvements anormaux (crise tonico-clonique focale) ou une paralysie des muscles d’un membre, de la tête, de la voix…
  • des troubles de la sensibilité (engourdissement, paresthésies)
  • des troubles d’apparence psychiatrique tels qu’une dysmnésie (flashbacks ou ecmnésie), des hallucinations psychotiques, une métamorphopsie (sensation de distorsion des objets) et des angoisses phobiques
  • des troubles du langage sur le versant expressif et/ou sur le versant réceptif : modifications du débit de parole, perte de l’intelligibilité, trouble de la compréhension…
  • des troubles du système nerveux végétatif :
    • tachycardie, hypotension, vomissements, diarrhées, dyspepsie (indigestion), hyper-salivation, gastralgies, reflux gastro-œsophagien.

Les crises partielles simples ne s’accompagnent pas de troubles de la conscience, à la différence des crises partielles complexes. Dans certains cas, les crises partielles peuvent se généraliser (tonico-cloniques) dans un second temps par extension à tout l’encéphale de la crise épileptique.

Syndromes épileptiques

Un certain nombre de syndromes épileptiques ont été individualisés, caractérisés par le contexte clinique, les symptômes épileptiques, et les résultats de l’électro-encéphalogramme.

  • Syndrome de West : affection grave touchant le nourrisson avant un an. Caractérisé par des spasmes, des troubles psychomoteurs avec mauvais développement intellectuel, et un électroencéphalogramme montrant une hypsarythmie typique. L’enfant gardera des séquelles neurologiques sévères, avec un bas pourcentage d’exception.
  • Syndrome de Lennox-Gastaut : affection grave touchant les jeunes enfants de deux à six ans. Des crises généralisées toniques ou des absences pluri-quotidiennes, des troubles intellectuels sont diagnostiqués. L’électroencéphalogramme entre deux crises est également typique. L’enfant gardera habituellement des séquelles neurologiques plus ou moins sévères. Cependant des cas rares peuvent évoluer sans séquelles.
  • Syndrome de Dravet, longtemps appelé « épilepsie myoclonique sévère du nourrisson » ou EMSN, comporte des crises convulsives sensibles à la fièvre qui peuvent être généralisées ou partielles. Il débute souvent entre 4 et 8 mois chez un nourrisson sans antécédent ni retard préexistant mais peut se déclencher plus tard, et qui n’accusera un retard que dans le courant de la deuxième année. L’épilepsie débute par des crises convulsives, unilatérales ou généralisées, spontanées ou provoquées par la fièvre, voire par un vaccin ; l’évolution est différente selon les cas mais souvent caractérisée par une instabilité du comportement, de la motricité, et un retard du langage. (source epilepsie France)
  • Épilepsie d’absence de l’enfant
  • Épilepsie myoclonique juvénile : maladie apparaissant à l’adolescence faite de crises myocloniques, avec un électro-encéphalogramme anormal. Évolution favorable. Elle se caractérise par des spasmes musculaires non contrôlés dont les signaux électriques du cerveau dure (généralement) quelques millièmes de seconde. Apparaissent, lors d’une crise longue de quelques minutes, certaines pertes sensorielles, dont l’impossibilité à trouver des mots permettant d’exprimer la pensée, ainsi que l’absence des sens spatio-temporels. À ce jour, aucun médicament ne peut arrêter formellement une crise épileptique myoclonique (juvénile ou non), mais quelques traitements permettent aujourd’hui l’atténuation des crises au fur et à mesure des années.
  • Épilepsie frontale à crises nocturnes
  • Convulsions fébriles de l’enfant : ces convulsions sont généralisées (tonico-cloniques) et apparaissent chez l’enfant, entre six mois et cinq ans, à l’occasion d’une hyperthermie, quelle qu’en soit l’origine — sauf pour la méningite qui est la cause directe des crises convulsives. Ces enfants ont une sensibilité supérieure aux autres enfants à faire des convulsions dans un contexte fébrile (lors d’une fièvre). Cette affection disparaît avec l’âge. L’électro-encéphalogramme est quasi-normal entre les crises.
Données anatomiques et fonctionnelles

Les données anatomiques permettent de mettre en évidence l’existence ou non de structures cérébrales endommagées et donc de connaître le foyer lésionnel susceptible de générer les crises d’épilepsie. Ces données sont enregistrées grâce à plusieurs modalités d’imagerie cérébrale telles que les images radiologiques, les scanners ou encore les Imagerie par Résonance Magnétique (IRM). De plus grâce aux progrès faits dans le domaine de l’imagerie encéphalique ces dernières années, il est aujourd’hui possible d’enregistrer les zones de fonctionnement de certaines parties du cerveau grâce à l’IRMf.

Modèles animaux de l’épilepsie

Étant donné que l’épilepsie semble être plus un groupe de symptômes qu’une maladie unique, plusieurs modèles sont utilisés pour étudier les mécanismes biologiques de l’épilepsie.

  • Une crise convulsive peut être provoquée chez de jeunes rats ou de jeunes souris (10 à 11 jours après la naissance) par une hyperthermie pendant 30 minutes afin de modéliser une crise fébrile. Chez certains rats (environ 30%), des crises focales peuvent être observées lorsqu’ils sont adultes.
  • Un état de mal épileptique (status epilepticus) peut être provoqué par l’injection intrapéritonéale de pilocarpine, un agoniste des récepteurs muscariniques ou celle de kaïnate, un agoniste des récepteurs glutamatergiques. Après un tel traitement, l’animal développe un profil EEG comparable à celui d’un état de mal épileptique chez l’homme et doit souvent être interrompu par l’injection d’une benzodiazépine (valium). Plusieurs semaines après cet état de mal, les animaux présentent des crises convulsives spontanées récurrente et des lésions dans l’hippocampe et d’autres structures limbiques qui évoquent une sclérose de l’hippocampe. Ces préparations, ou celles qui sont obtenues par l’injection dans l’hippocampe de kaïnate sont utilisées comme modèles d’épilepsie mésiotemporale.
  • Il existe aussi des animaux (rats, souris) qui possèdent une ou plusieurs mutations génétiques qui les rend épileptiques. En particulier, les GAERS (genetic absence epilepsy rat from Strasbourg) découverts à Strasbourg en 1982, présentent des crises d’épilepsie spontanées, non-convulsives caractérisées par un arrêt du comportement et la survenue de décharges de pointe-onde sur l’EEG. Ces crises et leur réactivité à certains antiépileptiques (valproate, éthosuximide) font du GAERS un modèle d’épilepsie absence 19. Une lignée de rats sans aucune crise a également été sélectionnée (NEC : Non Epileptic Control) à partir des mêmes animaux de départ (Wistar).
Corrélats biologiques

Pendant une crise épileptique, un grand nombre de neurones déchargent des potentiels d’action de manière synchronisée. La synchronisation des neurones est une propriété intrinsèque des réseaux neuronaux. L’observation d’EEG de sujets sains révèle l’existence de différentes fréquences propres à l’activité cérébrale qui correspondent à des synchronisations de groupes de neurones. Il semblerait que, dans le cas de l’épilepsie, cette synchronisation s’emballerait. Plus exactement, un dysfonctionnement se passe dans la transmission synaptique. Lors de cette transmission, des neurotransmetteurs ne partent pas de la terminaison pré-synaptique à la terminaison cible post-synaptique mais certains se rattachent à d’autres synapses. Ce phénomène est de l’ordre de 5 % à la normale, mais dans les épilepsies généralisées, il est de 25 %.

Plusieurs causes peuvent expliquer cet « emballement » :

  • une surexcitabilité des neurones ;
  • une diminution du niveau d’inhibition du réseau neuronal.

Une crise épileptique provoque sur chaque neurone concerné une série de changements qui peuvent expliquer qu’une épilepsie devienne chronique. Ces changements sont assimilables à la plasticité neuronale, laquelle explique aussi les processus de mémorisation et d’apprentissage.

L’inhibition neuronale semble contrôlée par une enzyme du métabolisme énergétique. Chez les épileptiques, ce contrôle pourrait être déficient, favorisant ainsi le déclenchement des crises.

Implication de la génétique

Il est vraisemblable qu’une multitude de gènes — dont beaucoup sont encore à identifier — interagissent de manière très complexe. Dans certaines formes génétiques familiales — concernant à peine 1 % des cas — des chercheurs australiens de l’Epilepsy Research Center de Melbourne (Australie) ont réussi à identifier une dizaine de gènes. Les recherches génétiques, qui se situent aux confins de la recherche et de la clinique, n’en sont qu’à leurs balbutiements, mais devraient pouvoir aider à l’avenir dans le diagnostic et le choix de certaines stratégies de traitements. Par exemple, dans le cas de certains types d’épilepsie, susceptibles de se compliquer d’une encéphalopathie chez de très jeunes enfants, les épileptologues espèrent pouvoir les diagnostiquer beaucoup plus tôt, dès les premiers mois de vie, grâce à la génétique moléculaire. Ceci, afin de pouvoir proposer un traitement capable de réduire la gravité de ces encéphalopathies, voire d’en empêcher la survenue.

En France, un centre de génétique moléculaire spécialement affecté à ces maladies rares a été mis en place à la Pitié-Salpêtrière.

Risques

L’épilepsie et les crises d’épilepsie ne mettent pas, en général, la vie de la personne épileptique en danger. Cependant, il est utile de mentionner quelques risques liés à l’épilepsie. La répétition des crises d’épilepsie peut entraîner l’apparition de lésions cérébrales. Ces lésions prédominent dans les régions cérébrales à l’origine des crises mais aussi dans une région particulière, la face interne du lobe temporal. Elles sont susceptibles par la suite d’être à l’origine de nouvelles crises — il est dit que la maladie s’auto-aggrave.

Lors d’une crise, le patient n’avale jamais sa langue, il est inutile (et dangereux) d’essayer de la retenir chez un patient en pleine convulsion.

Les risques liés à l’épilepsie ne concernent généralement pas la crise en elle-même, mais ses conséquences. Ainsi, si le patient conduit ou fait une mauvaise chute, à titre d’exemple, les conséquences de la crise peuvent alors être mortelles.

État de mal

L’état de mal épileptique engage le pronostic vital et fonctionnel (risque de séquelles neurologiques définitives). Elle est définie par une crise épileptique de durée anormalement longue (plus de 30 minutes), ou par la survenue de crises si rapprochées que le malade n’a pas le temps de recouvrer ses esprits entre deux crises. L’état de mal épileptique doit faire rechercher une cause déclenchante : arrêt du traitement, prise de toxiques (ivresse alcoolique en particulier), prise de médicaments contre-indiqués, infection, etc. Dans le cas d’un état de mal par crises convulsives tonico-cloniques, la durée de la crise fait craindre : insuffisance respiratoire par encombrement bronchique et bradypnée (ralentissement respiratoire), troubles circulatoires, séquelles neurologiques et intellectuelles définitives, troubles hydro-électrolytiques (déshydratation, acidose) et œdème cérébral.

L’état de mal peut aussi se produire dans le cadre du petit mal : un état confusionnel prolongé est alors retrouvé, associé à des manifestations cloniques du visage très évocatrices. En cas d’état de mal par épilepsie partielle, le diagnostic peut être difficile en raison de la ressemblance des symptômes avec ceux d’un accident vasculaire cérébral. L’électro-encéphalogramme permet de faire la différence. Dans les cas extrêmes, la crise peut conduire à la mort du patient, par anoxie cérébrale.

Spondylolisthésis par lyse isthmique

Le spondylolisthésis désigne une affection du squelette humain, caractérisée par le glissement d’une vertèbre en avant de la vertèbre située en dessous d’elle (antéspondylolisthésis) ou en arrière (rétrolisthésis).

Les vertèbres les plus souvent concernées sont la quatrième et la cinquième vertèbre lombaire.

Spondylolyse et spondylolisthésis isthmique chez l’adulte

La spondylolyse est une perte de continuité de l’isthme articulaire (pars interarticularis), situé entre les deux apophyses articulaires supérieure et inférieure de l’arc vertébral postérieur. Elle survient le plus souvent au niveau d’un étage vertébral lombaire bas, habituellement le dernier étage mobile. Elle peut être unilatérale ou bilatérale, induisant alors une micro mobilité ou une mobilité de l’arc postérieur. Elle peut être aiguë, traumatique, correspondant à un trait de fracture vrai, ou chronique, sans notion de vrai traumatisme. La perte de continuité s’organise alors sous la forme d’un tissu fibreux ou plus rarement pseudo-kystique plus ou moins hypertrophique dit « nodule de Gill », qui peut être agressif pour les racines nerveuses au contact. La lyse peut survenir dans l’enfance, mais aussi à l’âge adulte.

La fréquence de la spondylolyse au niveau lombaire est remarquablement élevée : de l’ordre de 3 à 7 % dans la population générale, beaucoup plus dans certains groupes. Si Inuits et Bushmen sont classiquement des groupes à risque, la fréquence des spondylolyses est de 14 % chez les athlètes de haut niveau, particulièrement 20 % chez les danseurs, et de 11 à 17 % chez les gymnastes et les rameurs, au point que la constatation d’une spondylolyse puisse être considérée comme presque physiologique dans certains groupes de sportifs…

Le spondylolisthésis est un déplacement permanent du corps vertébral en avant sur le corps vertébral sous-jacent, constituant un antéspondylolisthésis, ou en arrière (rétrolisthésis). Il est deux à trois fois moins fréquent que la spondylolyse isthmique. Dans sa forme dite isthmique, il survient à la faveur d’une spondylolyse vraie, ou d’un allongement « dysplasique » de l’isthme sans perte de continuité qui est peut-être le résultat de lésions traumatiques consolidées. Les spondylolisthésis ont été classés de façon purement descriptive par Newman en 5 types essentiels.

  • Le type isthmique est le type II, avec une forme lytique IIA, une forme avec allongement de l’isthme sans lyse IIB, et une forme traumatique aiguë avec fracture des isthmes IIC.
  • Le type I « dysplasique » et plutôt rare recouvre un ensemble de malformations congénitales de la charnière lombo-sacrée : incompétence des articulaires postérieures dysplasiques associée à une anomalie de croissance du sacrum « en dôme », il se voit chez l’enfant et s’accompagne de troubles radiculaires car l’arc postérieur est habituellement intact.
  • Le type III correspond au spondylolisthésis dit « dégénératif » : il s’agit d’un glissement habituellement à l’avant dernier niveau mobile, dû à la faillite arthrosique des apophyses articulaires postérieures et permise par la dégénérescence discale associée. Ceci survient chez un individu âgé au moins sur le plan physiologique, et s’accompagne de signes radiculaires au premier plan, car l’arc postérieur reste en continuité du corps, et l’effet « coupe-cigare » ajouté à l’hypertrophie arthrosique des articulations inter-apophysaires crée un syndrome canalaire de type claudication neurologique ou de type radiculalgique, selon la prédominance globale ou latérale de la sténose. Le déplacement lui-même est habituellement modéré.
  • Le type IV intéresse le glissement acquis à la suite de la rare fracture traumatique des apophyses articulaires.
  • Le type V comprend les conditions pathologiques locales (infection, tumeur) ou générales conduisant à la destruction des facettes, pédicules ou isthmes.
  • Enfin le type VI, ajouté ultérieurement, est le spondylolisthésis créé par la destruction chirurgicale de l’arc postérieur.
Physiopathologie

Les facteurs locaux sont essentiels : hyper lordose constitutionnelle, répétition de mouvements en hyper-lordose, angle d’incidence élevé, apophyses articulaires inférieures de grand volume à l’avant dernier niveau mobile, mettent l’isthme aplati du dernier niveau mobile en danger de cisaillement avec les apophyses articulaires sacrées à la faveur d’un traumatisme aigu ou chronique.

Plateau sacré arrondi « en dôme », incidence élevée, sont des facteurs d’aggravation du glissement.

Des facteurs congénitaux et héréditaires inconnus ont été évoqués pour expliquer la fréquence accrue dans certaines populations et certaines familles, sans qu’on connaisse le rôle de la posture et de l’habitus.

La spondylolyse serait une pathologie de la marche, inconnue chez les patients non ambulatoires, bien que des cas aussi précoces qu’à l’âge de 2 ans aient pu être décrits.

Lorsque l’isthme est rompu ou allongé de façon bilatérale, le corps vertébral libéré du contrôle de l’arc postérieur soumet le disque sus-jacent et les ligaments ilio-lombaires à la totalité des contraintes de cisaillement qu’il subit. Des contraintes en cisaillement et de la capacité de résistance de l’anulus dépendent la constitution ou non d’un spondylolisthésis.

Spondylolyse et spondylolisthésis isthmique sont des aspects différents d’une affection dont la variabilité clinique est remarquable.

Il y a des spondylolyses bien tolérées sur de très longues périodes sans spondylolisthésis, des spondylolisthésis sans spondylolyse, des spondylolisthésis stables non évolutifs pendant de nombreuses années, des formes d’aggravation lente ou rapide qu’il faut détecter à temps, et des formes mixtes. Il n’y a donc pas de filiation stricte entre les deux états et seule la surveillance est à même d’affirmer l’évolutivité vers l’aggravation du déplacement vertébral.

Les facteurs de progression sont : le sexe féminin, l’obésité, les contraintes en hyper lordose, l’âge (adolescents en période de croissance), la cyphose locale.

Le glissement constitué, le corps vertébral subit deux types de déplacements : le glissement vers l’avant proprement dit, la bascule en cyphose. S’y ajoute le déplacement vers le bas par effet de pente, et la ptose lorsque le corps vertébral échappe en bout de course au support du plateau vertébral érodé sous-jacent, sous l’effet du poids du tronc et de la traction du psoas sur le rachis lombaire.

Quantification du glissement

L’index de Taillard mesure le glissement à partir du repère du coin postéro-inférieur de la vertèbre olisthésique, en pourcentage de la longueur antéro postérieure du plateau sacré sous-jacent. En France, on divise traditionnellement le plateau sacré en trois tiers dans le sens antéropostérieur, et on cote le glissement antéropostérieur en fonction de l’épaisseur de ce plateau :

  • Grade 0 (pas de glissement, ou spondylolyse sans glissement)
  • Grade I glissement inférieur à 1/3 du plateau vertébral
  • Grade II de 1/3 à 2/3, bord postérieur du corps vertébral en regard du milieu du plateau sacré
  • Grade III plus de 2/3
  • Grade IV glissement complet au-delà de la limite antérieure du plateau sous-jacent avec spondyloptose

Dans le monde anglo-saxon, à partir de la même référence (Meyerding), on divise le plateau sacré en quatre quarts et il y a 5 stades numérotés de I à V… Cependant, on s’accorde sur le fait que les spondylolisthésis dont le glissement (index de Taillard) est inférieur à 33 % ont une évolution et des implications thérapeutiques différentes de ceux dont le glissement est plus important. Dans les spondylolisthésis de haut grade, la partie antérieure du plateau vertébral érodée prend un aspect arrondi ou oblique, avec un plateau à double pente, qui rend la mesure de l’index de Taillard peu précise. Il existe une spondyloptose lorsque le coin postéro-supérieur du corps vertébral migré se trouve en position debout plus bas que le coin postéro-supérieur du plateau vertébral sous-jacent quel que soit le déplacement angulaire.

Clinique

Il existe en pratique 3 formes cliniques bien différentes : la spondylolyse isolée, le spondylolisthésis grade I, les spondylolisthésis grade II et III. La spondyloptose pose quant à elle des problèmes très particuliers.

Spondylolyse isthmique – Clinique

Le tableau complet est fait de douleurs lombaires diurnes ou nocturnes mais plutôt mécaniques, de radiculalgies et pseudo radiculalgies de topographie S1 plutôt que L5, siégeant dans la face postérieure des cuisses et souvent tronquées au genou, de troubles de la statique avec rétraction des ischio jambiers, dont l’origine précise est inconnue. Il est rare, mais évocateur chez un adolescent ou un adulte jeune. En pratique, nombre de spondylolyses sont de découverte systématique en l’absence complète ou presque complète de symptomatologie. Le problème est plutôt de déterminer la responsabilité d’une lyse isthmique bien banale chez un adulte lombalgique chronique afin d’éviter une chirurgie qui ne résoudra pas le problème douloureux.

Cliniquement, on recherche un trajet radiculaire vrai, un Lassègue, l’existence d’un déficit et d’une rétraction des ischio jambiers que l’on cote en mesurant l’angle poplité à 90° de flexion de cuisse en position couchée.

Spondylolyse isthmique – Imagerie

Faire le diagnostic : les clichés standard peuvent montrer la lyse à un œil entraîné, les clichés centrés de 3/4 font toujours partie de l’arsenal diagnostic à la recherche de la décapitation du petit chien radiologique de Lachapelle. Les coupes de scanner peuvent aider mais peuvent aussi passer dans le plan de la lyse et être difficiles à interpréter, quelquefois ce sont seulement les reconstructions tridimensionnelles dans le plan des isthmes qui permettent de trancher. Dans certaines formes infra radiologiques en particulier chez le jeune sportif lombalgique, la scintigraphie osseuse au Tc 99 peut faire suspecter la lyse en montrant une fixation uni ou bilatérale. La scintigraphie permet également de suspecter le caractère récent d’une lyse constituée chez un patient jeune. Le diagnostic précoce a un intérêt si on peut par un traitement précoce (diminution des activités, immobilisation) éviter de passer au stade de lyse radiologiquement constituée. Chercher autre chose : chez un adulte lombalgique chronique ou qui se plaint de radiculalgies, la lyse isthmique est l’arbre qui cache la forêt … hernie discale intra ou extra canalaire, au même niveau ou à un autre niveau, tumeurs rachidiennes voire ostéome ostéoïde sont des diagnostics associés possibles, en marge de la lombalgie essentielle d’origine discale pure dont la physiopathologie et les indications thérapeutiques restent discutées. Bilan préthérapeutique : L’IRM montre le volume du “ nodule de Gill ” , une anomalie radiculaire associée, une hernie discale au même niveau (en se méfiant des effets de volume partiel qui sont beaucoup plus fréquents), l’état du disque, et celui du disque sus jacent [59] dans une perspective chirurgicale.

Spondylolyse isthmique – Formes cliniques

La spondylolyse aiguë post traumatique, peut être unilatérale, il s’agit d’une vraie fracture en hyper extension et rotation du tronc, elle justifie un traitement conservateur prolongé dont le but est l’obtention de la consolidation et la restitution ad integrum. Devant une lyse constituée dans un cadre traumatique, la scintigraphie permet d’affirmer le caractère récent et de traiter en conséquence. L’immobilisation par corset est contraignante, car elle nécessite de prendre une cuisse de façon permanente.

Les spondylolyses strictement asymptomatiques ne justifient pas d’autre traitement qu’une surveillance d’autant plus rapprochée qu’il s’agit d’un individu jeune surtout chez l’adolescent sportif. En particulier, il n’y a pas de nécessité d’interdire les activités sportives. Il faut revoir le patient tous les trois à six mois initialement afin d’évaluer la stabilité. Le facteur d’évolutivité essentiel est le jeune âge du patient, enfant ou adolescent.

Indications thérapeutiques

Les lombalgies pures sont en général accessibles au traitement médical assorti d’exercice quotidien. Le but est de maintenir et renforcer la tonicité des muscles spinaux, et de lutter contre l’apparition d’une rétraction des ischio jambiers. Le traitement chirurgical se discute en fonction de la gêne provoquée : fréquence des épisodes de lombalgie récurrente, présence de radiculalgies, rétraction des ischio jambiers.

Techniques chirurgicales

La réparation directe du défect par greffon isthmique et instrumentation spécifique sans arthrodèse s’adresse à des patients qui ne nécessitent pas d’exploration canalaire donc sans radiculalgies vraies, qui ont un disque sous-jacent en bon état vérifié par l’IRM, et un défect isthmique de petit volume accessible en extra canalaire à un greffon osseux. Avec un tel niveau d’exigence, peu de patients justifient la chirurgie, et les indications sont limitées dans la forme actuelle. L’arthrodèse postéro-latérale non instrumentée (Wiltse) est réalisée par une double voie postéro-latérale entre longissimus et multifidus, les greffons de crête iliaque sont apposés au contact des transverses et articulaires de L4 à l’aileron sacré avivés. L’immobilisation postopératoire en appareil de contention est à mettre en œuvre jusqu’à consolidation, habituellement 3 mois. L’arthrodèse L5 S1 instrumentée après libération canalaire : après exposition et résection de l’arc postérieur mobile, on excise de façon bilatérale le nodule fibreux au contact de la racine L5 et on complète la libération par la régularisation de la partie basse du pédicule L5 qui a fréquemment une forme en crochet agrippant la racine. Une instrumentation pédiculaire est mise en place de L5 à S1 et l’arthrodèse réalisée de la transverse de L5 à l’aileron sacré après un avivement qui doit être soigneux. L’arc postérieur réséqué peut fournir assez de greffons, cependant la fréquence des non-consolidations est fonction inverse du volume et de la qualité de la greffe, ce qui justifie la prise de greffe iliaque en sous aponévrotique par la même voie d’abord. Combinaisons : la voie postéro-latérale de Wiltse permet au besoin de mettre en place une instrumentation pédiculaire qui soutiendra la greffe en cas d’hyper mobilité. L’arthrodèse postéro-latérale instrumentée peut être réalisée sans exploration endocanalaire et sans résection de l’arc postérieur, en fonction des besoins d’exploration et de stabilisation. Les données qui entrent dans le choix technique sont essentiellement l’âge (consolidation plus facilement obtenue chez l’adolescent que chez l’adulte [118], qui fait préférer une arthrodèse instrumentée), la nécessité d’une exploration endocanalaire (radiculalgies vraies, conflit endocanalaire concordant) et l’état du disque sus-jacent vérifié sur l’IRM. La dégénérescence de celui-ci engage à étendre l’arthrodèse à l’avant dernier niveau mobile.

Gastro-entérite

Une gastro-entérite est une infection inflammatoire du système digestif pouvant entraîner de la nausée, des vomissements, des crampes abdominales, des flatulences et de la diarrhée, ainsi que de la déshydratation, de la fièvre et des céphalées (maux de tête).

La gastro-entérite peut être d’origine bactérienne, c’est-à-dire due à la consommation d’eau ou de nourriture contaminée par des bactéries, telles que les colibacilles présents dans les selles. Des symptômes de gastro-entérite peuvent aussi être dus à des parasites internes, protozoaires ou amibes pathogènes, tel qu’Entamoeba histolytica provoquant la dysenterie amibienne ou amibiase généralement due à des installations sanitaires absentes ou inadéquates.

Cependant, dans plus des deux tiers des cas, elle est causée par des virus comme les rotavirus, (provoquant en particulier la gastro-entérite infantile), les norovirus (dont le virus de Norwalk), les adenovirus, des calicivirus et des astrovirus. La gastro-entérite est communément appelée « grippe intestinale » (terme inadéquat mais très répandu), lorsqu’elle est causée par un virus, et « empoisonnement alimentaire » ou plus justement « intoxication alimentaire » lorsque causée par une bactérie.

La gastro-entérite peut également révéler une dysenterie des voyageurs, aussi connue sous le terme de diarrhée du voyageur ou tourista. Celle-ci peut être due à une infection, le plus souvent par des bactéries (notamment Salmonella, Aeromonas, Escherichia coli, Campylobacter, Shigella, Vibrio cholerae (causant le choléra) et Vibrio (non cholérique). Parfois, l’infection peut provenir de virus, norovirus (principalement virus de Norwalk), adénovirus, astrovirus, entérovirus, rotavirus. Plus rarement, la tourista sera causée par des amibes ou protozoaires parasitaires (Cyclospora, Entamoeba histolytica, Cryptosporidium, Giardia ou autre parasite intestinal).

La diarrhée s’accompagne souvent de vomissements et de poussées de fièvre, mais les symptômes varient en fonction des individus. En effet, certains se contentent de vomir, d’autres n’ont aucun symptôme, et certains n’ont que la diarrhée. Si elle est trop importante, elle peut mener à une déshydratation de l’organisme.

Si la diarrhée perdure, elle peut laisser des séquelles sur la paroi intestinale, menant à une pathologie appelée syndrome de malabsorption.

Épidémiologie

Le rotavirus est la cause la plus courante de diarrhée et de déshydratation chez l’enfant, en particulier dans les pays développés. Dans le monde, on estime que 125 millions de diarrhées sont provoquées annuellement par ce virus (soit plus de 1 900 cas pour 100 000 habitants). On estime que chaque année, 800 000 personnes meurent de gastro-entérite dans le monde, dont 500 000 enfants de moins de cinq ans, ce qui représente 25 % des morts par diarrhées et 6 % des morts de moins de cinq ans.

Aux États-Unis, on estime que le rotavirus touche 80 % des enfants de moins d’un an ; chaque année, 500 000 enfants doivent faire l’objet de soins médicaux, et 50 000 doivent être hospitalisés.

En France, lors du pic de l’épidémie hivernale 2005–2006, on estime que 1 850 000 personnes ont consulté leur médecin généraliste en 8 semaines pour une gastro-entérite ; l’incidence a été de 367 cas pour 100 000 habitants (le seuil épidémique étant fixé à 279 cas pour 100 000 habitants). La surveillance de l’évolution de l’incidence en France est effectuée par le réseau Sentinelles de l’Inserm qui publie ces données, comme une société de communication spécialisée qui met aussi ces données à la disposition du public.

Il s’agit donc d’un important problème de santé publique. D’autant que chaque année, l’épidémie de gastro-entérite à rotavirus concorde souvent avec les épidémies de bronchiolite et de grippe, pouvant mettre en difficulté les systèmes de soins pédiatriques.

On peut remarquer que les gastro-entérites virales sont en recrudescence pendant l’hiver, surtout en Amérique du Nord et en Europe.

Diagnostic

Les symptômes habituels de la gastro-entérite sont des nausées, la perte d’appétit, crampes abdominales et vomissements qui apparaissent brutalement, de la diarrhée, de la fièvre et des céphalées (maux de tête). Plus rarement, des vertiges et une hypotension peuvent accompagner les symptômes, sans doute liés à la déshydratation et à la fatigue.

Les symptômes communément associés à la gastro-entérite, c’est-à-dire principalement les vomissements et la diarrhée, peuvent également être signes d’un empoisonnement (fruits de mer, champignons toxiques) ou d’infections systémiques (pneumonie, septicémie, etc.). Par un interrogatoire précis et le contexte clinique, il sera possible d’éliminer ces hypothèses.

La gastro-entérite peut parfois déboucher sur des complications telles que la déshydratation, pouvant même conduire à une hospitalisation. Les personnes à risque sont les jeunes enfants et les nourrissons, les personnes âgées, et les personnes ayant un système immunitaire affaibli par une maladie (VIH par exemple). Les signes de la déshydratation sont une sécheresse de la peau et de la bouche, les yeux et les parties molles du crâne (chez les nourrissons) enfoncées, des faiblesses, crampes, et perte de poids, et des urines moins fréquentes et plus foncées que d’habitude.

Si l’on suspecte une gastro-entérite d’origine bactérienne, il est possible d’effectuer une analyse des selles au laboratoire (coproculture) à la recherche de la bactérie en cause.

Génétique

Une mutation sur le gène FUT2 (en), présente chez 20 % des Européens, confère une haute résistance, voire une immunité, contre le norovirus, responsable à 85 % des gastro-entérites non bactériennes, en dehors du jeune enfant.

Antibody List

1-21.2 cAMP-specific phosphodieserase PDE4A4
10.1.1 Chloride channel calcium activated 3A1; CLCA1 protein
103BF1.1 Tannerella forsythia, strain FDC 331 (OMZ 348)
10C1 (reovirus) reovirus outer capsid protein sigma 3
10C9 anti-late bloomer late bloomer
10D3 anti-wrapper wrapper
10E5 integrin alphaIIb
10F1 ecdysone receptor (EcR) (common), Manduca sexta
10F5 myosin heavy chain, fast, 2B
10F6 (reovirus) reovirus capsid protein mu 1C
10G10 (reovirus) reovirus outer capsid protein sigma 3
116BF1.2 Tannerella forsythia, strain FDC 331 (OMZ 348)
12-120-94/6 csA (contact site A glycoprotein)
12/101 skeletal muscle marker, 102 kDa
12/21/1-C-6 proteoglycan, hyaluronic acid binding region; aggrecan
123-353-1 csA (contact site A glycoprotein)
12A7 Frizzled2
12C5 versican (hyaluronate-binding region)
12F10-5F11 Megator
12G10 anti-alpha-tubulin tubulin (alpha-)
12G9 filament antigen
130-80-2 crystal protein
132-250-1 Peptide II B 80kD
135-409-16 Cap32/34
138AA1.1 Aggregatibacter actinomycetemcomitans serotype c
13C9 anti-Robo Robo (Drosophila)
13F4 muscle marker
13G3B7 Fibronectin III-15 fibronectin (III-15)
141AA1 Aggregatibacter actinomycetemcomitans serotype b
145AA1.1 Aggregatibacter actinomycetemcomitans serotype b
14A3D2 Mmp1 hemopexin domain
14C9 anti-Robo3 extracellular Robo3 extracellular (Drosophila)
14a9 nuclear lamins II/III (Xenopus)
14h7 vimentin (Xenopus)
15.3B9(NOT1) notochord marker
150AA1.1 Aggregatibacter actinomycetemcomitans serotype a
151-IgG or 151-8 AE4 epidermal growth factor receptor
151AA1.2 Aggregatibacter actinomycetemcomitans serotype a
159-183-10 Proteasome subunit
159-291-1 actin binding protein 34 (ABP34)
15AE10 integrin beta-3 (CD61), human
15C3 ecdysone receptor (EcR) (common), Manduca sexta
15F12F8 ribosome, 30S (E. coli)
15G1a(EcR-A) ecdysone receptor (EcR-A)
15H2 anti-Robo3 cytoplasmic Robo3 cytoplasmic (Drosophila)
16-3C1 transketolase
16.5H2 neuronal, motor, marker (SC-1)
169-477-5 talin
169-90-2 actin binding protein 34 (ABP34)
16B2B1 ribosome, 30S (E. coli)
17.1G6 cardioactive peptide B
171-337 Proteasome subunit 5
176-2-5 coronin
176-3-6 coronin
177-29-B2/5 Coactosin p17
179ME1 Mutanase G
191ME1 Mutanase G
193E11E5B11 ribosome, (E. coli)
193F10C8C11 ribosome, (E. coli)
194-62-6 Coronin N-terminal
195ME3 Mutanase G
19C2 anti-Sema II Sema II
1A1-3C2 Skeletor
1A10 oncomodulin (beta-parvalbumin)
1A8 Us9 (pseudorabies virus)
1B1 hu-li tai shao, not hts-PC
1B11 GPI-linked Neurocan receptor neurocan receptor
1B2 JW hexokinase (Type I isozyme)
1B5 integrin alphaIIb/beta-3 (CD61) complex, mouse
1B6-C4 blastema, regenerating
1C10 HNK-1 epitope
1C11 Frizzled protein
1D1 neurocan (C-terminal epitope)
1D10 CD44
1D12 Gurken protein
1D4 anti-Fasciclin II fasciclin II (Drosophila)
1D4B LAMP-1 (110 kDa lysosomal membrane glycoprotein)
1D8 (reovirus) reovirus sigma NS
1D9-E11 blastema, regenerating
1E11 synaptotagmin B
1E12 actinin, smooth muscle alpha
1E8 Schwann cell marker, P(o) (avian)
1F6 neurocan (N-terminal epitope)
1G12 nidogen/entactin
1G2 FXR2
1G9 hindsight protein
1H6-E9 blastema, regenerating
1H9 Fibronectin Hep2 / 1H9B2 fibronectin (III-14 in Hep2)
1h5 cytokeratin type II (Xenopus)
20-121-1 csA (contact site A glycoprotein)
20-53-1 csA (contact site A glycoprotein)
200MH1 Mutanase G
20B4 neural crest cells
20H5 Cdk7, recombinant
21-55-4 myosin II heavy chain
21-96-3 myosin II heavy chain
210-183-1 Fimbrin (p67)
210-287-3 Fimbrin
212WR2 Campylobacter rectus
21A6 retinal space (mechanoreceptors?)
22/18 blastemal regeneration cell marker of the newt
224-236-1 actin
224-256-2 V_H_ATpase c-subunit
227-341-4 talinA (N-terminal)
22B12B2 30S ribosomal protein S3
22C10 futsch
22d4 mannose 6-phosphate receptor, cation-dependent
23-132-27 calmodulin
23.4-5 neuronal marker (TAG-1)
232-238-10 Cortexillin II
232-238-8 Cortexillin II
23A7 (anti NrCAM) NrCAM
23C7 anti-wit wit
23E9E7 ribosome, 30S (E. coli)
24 ATPase, (Na(+) K(+)) beta-subunit
24-210-2 csA (contact site A glycoprotein)
241-438-1 Cortexillin I
248AA4.4 Aggregatibacter actinomycetemcomitans serotype e
24B10 chaoptin, sensory neurons
252-234-2 calreticulin, recombinant Dictyostelium
260AA3 Aggregatibacter actinomycetemcomitans serotype a´
261AA2.2 Aggregatibacter actinomycetemcomitans
262AA1.1 Aggregatibacter actinomycetemcomitans serotype a´
266AA1 Aggregatibacter actinomycetemcomitans serotype e
26E4C7 PTP-ER
270-390-2 Calnexin
28F12 TSLP
2A1 Cubitus interruptus
2A12 tracheal system; GASP
2A4 hexokinase (Type I isozyme)
2A9 (reovirus) reovirus sigma NS
2B10 Cut protein product
2B49 phosphacan/protein tyrosine phosphatase – z/b
2B6 hexokinase (Type I isozyme)
2B8 even-skipped protein
2B9 collagen type IX
2C11-2 dynein heavy chain
2C2 collagen type IX
2C4-C2 blastema, regenerating
2C6 alpha-2-macroglobulin receptor
2D5 MHC class II
2D7F8 PTP-ER
2E8 laminin
2E9 myosin heavy chain, neonatal fast
2F4 myosin heavy chain, fast, jaw muscle specific
2F4 (reovirus) reovirus sigma 1s
2F5 (reovirus) reovirus sigma NS
2F5-1 FMRP (residues #1-204)
2F7 myosin heavy chain, fast, 2A
2G9 LAMP (gene symbol: Lsamp)
2H3 Neurofilament (NF-M)
2H7 (reovirus) MBP-sigma NS-His
2H8 CD31 (PECAM-1)
3.1C12 neuronal marker (TAG-1)
31 or 31-2 laminin
32-5B6 S-adenosylhomocysteine hydrolase
325AA2 Aggregatibacter actinomycetemcomitans
326PM2 Parvimonas micra
328AA2.2 Aggregatibacter actinomycetemcomitans serotype d
33 or 33-2 heparan sulfate proteoglycan
33-294-17 csA (contact site A glycoprotein)
330AA3.2 Aggregatibacter actinomycetemcomitans serotype d
341AN3 Actinomyces oris
34B3 anti-Fasciclin II fasciclin II (Drosophila, all isoforms)
34C Ryanodine receptor
37-1A9 Xenopus nuclear factor, xnf7
37-1B2 transketolase
371D12F6 ribosome, 30S (E. coli)
373C9C3A1 ribosome, 30S (E. coli)
389C6G7B9 ribosome, 30S (E. coli)
39 collagen type VI
39.3F7 Islet-1 specific homeobox
39.4D5 Islet-1 & Islet-2 homeobox
390C3F1D3 ribosome, 30S (E. coli)
391B9E4E1 ribosome, 30S (E. coli)
396AN1 Actinomyces naeslundii, oris and israelii
397AN1.1 Actinomyces naeslundii and oris
39BI1.1.2 Prevotella intermedia and nigrescens (cell surface antigen)
3A10 neurofilament-associated antigen
3A6 protein tyrosine phosphatase, receptor-linked, DPTP99A
3A6B4 Mmp1 catalytic domain
3A9 (323 or M10-2) spectrin, alpha
3B11 anti-grasshopper Fas I fasciclin I (grasshopper)
3B2 collagen type III
3B3 decorin
3B5 AP-2 alpha
3B8D12 Mmp1 catalytic domain
3C10 anti-even skipped even-skipped protein (Drosophila)
3C11 (anti SYNORF1) synapsin
3CB2 radial glial cells / vimentin
3E10 (reovirus) reovirus sigma NS
3E2 (reovirus) MBP-sigma 1s
3F11 protein tyrosine phosphatase 69D
3F2/D8 Podocalyxin/gp135
3F8 phosphacan/protein tyrosine phosphatase – z/b
3H1 keratan sulfate (brain)
3H11 laminin
3H1D8F5 anti-gigas gigas gene product
3H2 2D7 synaptotagmin
3H5 HNK-1 epitope
3gA2 lysine decarboxylase (E. corrodens)
3hE5 lysine decarboxylase (E. corrodens)
4-34.10 cAMP-specific phosphodieserase PDE4A4
40-1a beta-galactosidase
40.2D6 Islet-1 homeobox
40.3A4 islet-1 homeobox
40BI3.2.1 Prevotella intermedia (cell surface antigen)
40E-C radial cells and radial glial cells (vimentin)
421AG1 Actinomyces naeslundii and oris
455-2A4 Transcription factor elt-2
45E10 protein tyrosine phosphatase, receptor-linked, DPTP10D
47-18-9 alpha-actinin
47-60-8 actinin, alpha-47-60-8
47-62-17 alpha-actinin
49BG1.3 Porphyromonas gingivalis (cell surface antigen)
4A3 (reovirus) reovirus capsid protein mu 1C
4A5 major sperm protein (MSP)
4A6 myosin heavy chain, fast, extraocular specific
4A6 JW hexokinase (Type I isozyme)
4B12 Fibronectin
4B5.13 cAMP-specific phosphodieserase PDE4A8
4C1 transglutaminase, tissue
4C5 rhodopsin 1 (Rh1 Drosophila)
4C7 HNF3b / FoxA2
4C71B7 protein tyrosine phosphatase, receptor-linked, DPTP99A
4C9H4 anti-peanut peanut gene protein product
4D4 Wingless protein
4D6 collagen type IX
4D7/TAG1 neuronal marker (TAG-1)
4D9 anti-engrailed/invected engrailed/invected gene products
4E1.16 cAMP-specific phosphodieserase PDE4A8
4E2(3G2) neuromuscular junction and reactive Schwann cell associated antigen
4F12 sialomucin complex (Muc4)
4F2 Lim 1+2 / LhxV5
4F2 (reovirus) reovirus
4F3 anti-discs large discs large (Drosophila)
4G1 MSX1+2
4G11 Engrail-1
4H2 Fibronectin
4H6 neurofilament (NF-M)
4d NCAM (cytoplasmic domain)
5-13.4 cAMP-specific phosphodieserase PDE4D5
5-14 myosin heavy chain A
5-23 paramyosin
5-6 myosin heavy chain A
5.1H11 NCAM
50.5A5 LMX
51.4H9 Islet-2
54-11-10 Hisactophilin, Dd gelation factor
56-396-5 Myosin II
56.4H7 rhoB
5A3 hexokinase (Type I isozyme)
5A5 NCAM (sialylated form); PSA-NCAM
5A6 tau
5B1-E6 blastema, regenerating
5B5-2 Hoxc9
5B8 NCAM
5C2 hexokinase (Type I isozyme)
5C3 (reovirus) reovirus outer capsid protein sigma 3
5C6 collagen type VI
5C6 (reovirus) reovirus
5C9 perlecan (domain IV)
5D2-27 Pgp-1 (Ly-24) lymphocyte cell adhesion glycoprotein
5D3 cadherin, E-
5E1 sonic hedgehog
5E12-E3 blastema, regenerating
5E4 AP-2 alpha
5F10 allatostatin (Ast7)
5G10 lysosomal membrane glycoprotein (LEP-100) / CD107
5G12-10 Hoxc10
5G2 anti-enabled enabled
5H7B11 Mmp1 catalytic domain
5e NCAM (extracellular domain)
602.29 cl. 11 chromosome 12, 21 kDa product
60BG1.3 Porphyromonas gingivalis, strain W83 (OMZ 309)
61BG1.3 Porphyromonas gingivalis, strain W83 (OMZ 309)
62.1E6 Slug
65B12 TSLP
67.4E12 Lim 3
6B3 Cadherin, N- (neural)
6B6 cadherin, C-
6B7 ecdysone receptor (EcR) B1-isoform specific, Manduca sexta
6B9 Villin-like protein quail; 6B9
6C4 collagen type XVIII
6C8-A2 blastema, regenerating
6D1 GPIb; von Willebrand factor receptor; GPIb/IX complex
6D2 agrin
6D6 decorin
6E8 Posterior sex combs protein
6F1 integrin alpha-2; alpha2beta1 integrin complex
6F8 anti-grasshopper Sema I Sema I (grasshopper)
6G10-2C7 blastema, regenerating
6G7 tubulin
6H1 myosin heavy chain, fast, 2X
6H4 anti-highwire highwire
70-100-1 porin
72.5B10 ER81
74.5A5 Nkx2.2
7A1 (reovirus) reovirus outer capsid protein sigma 3
7A2 GPI-linked Neurocan receptor neurocan receptor
7A6 NFATc1
7B1 decorin
7B11 cyclic nucleotide-gated channel (rOCN2, rat)
7D6 L-CAM, E-cadherin, uvomorulin
7E2 integrin beta-1
7E9 fibrinogen
7F4 (reovirus) reovirus gamma 2 vertex protein
7G1-1 FMRP
7G10 anti-Fasciclin III fasciclin III (Drosophila)
7G4 visinin
7H2 integrin beta-3
8.1.1 stromal cell line (murine)
80-52-13 Discoidin I (cAMP binding domain)
81.5C10 MNR2/HB9/Mnx1
86f7 mannose 6-phosphate / IGF II receptor, cation-independent
8A2 neural associated ganglioside
8B22F5 protein tyrosine phosphatase, receptor-linked, DPTP10D
8B4D2 (MH2B) glutamate receptor subunit, DGluR-IIA
8C2 cadherin, E-
8C3 syntaxin (Drosophila)
8C6 anti-grasshopper Fas II fasciclin II (grasshopper)
8C8 integrin beta-1 (Xenopus)
8D12 anti-Repo Repo
8D9 L1-like CAM (avian)
8F12 (reovirus) reovirus outer capsid protein sigma 3
8F3 chicken cell marker
8H1 (reovirus) reovirus sigma NS
8H6 (reovirus) reovirus capsid protein mu 1C
8H9 CD64
8e6 talin (avian)
9 D10 titin
9.1 ITGA7 Integrin alpha-7, extracellular domain
9.4A anti-Trio Trio
9/30/8-A-4 link protein
99.1-3A2 Evx1
9B2.1 anti-glass glass Drosophila protein
9B8 anti-sidestep sidestep
9B9 ecdysone receptor (EcR) (common), Manduca sexta
9BA12 chondroitin sulfate proteoglycans (carbohydrate epitope)
9D82B3 DLAR
9E 10 c-myc
9H5 integrin beta 3
9H6 entactin (synaptic)
9S4 Selenoprotein P
A12 cyclin A
A21F7 integrin alpha-5  (avian)
A2B11 transitin
A4.1025 myosin (human all fibers)
A4.1519 Myosin heavy chain (human nascent secondary and all fast fibers)
A4.74 Myosin heavy chain (human fast fibers)
A4.840 Myosin heavy chain (human slow fibers)
A4.951 Myosin heavy chain (human slow fibers)
A6 BCM A6 antigen in biliary epithelial/oval cells
A72-24 phosphatidylinositol-specific phospholipase C
AA12.1 tubulin (beta-)
AA4.3 tubulin (alpha-)
AB8 myosin heavy chain, adult
ABL-93 LAMP-2 (110 kDa lysosomal membrane glycoprotein)
ABP2 ABP2 olfactory binding protein
AC4 neural tube, dorsal
AD4.4(EcR-B1) ecdysone receptor (EcR-B1)
ADL101 lamin Dm0
ADL195 lamin Dm0
ADL40 lamin Dm0
ADL46 lamin Dm0
ADL67.10 lamin Dm0
ADL84.12 lamin Dm0
AE-2 acetylcholinesterase
AF-CA2 Aspergillus flavus isolate 93803
AFFN-AKT3-10E3 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-10F2 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-13B4 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-16B3 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-18F11 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-1B9 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-1H11 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-20A3 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-2F10 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-7H5 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-8F3 RAC-gamma serine/threonine-protein kinase
AFFN-AKT3-9F4 RAC-gamma serine/threonine-protein kinase
AFFN-APLF-15F11 Aprataxin and PNKP like factor
AFFN-APLF-4H5 Aprataxin and PNKP like factor
AFFN-ARHGC-1-15A6 Rho guanine nucleotide exchange factor (GEF) 12
AFFN-ARHGC-1-2B12 Rho guanine nucleotide exchange factor (GEF) 12
AFFN-ARHGC-1-9H2 Rho guanine nucleotide exchange factor (GEF) 12
AFFN-ARHGEF12-15D11 Rho guanine nucleotide exchange factor (GEF) 12
AFFN-ARHGEF12-17B8 Rho guanine nucleotide exchange factor (GEF) 12
AFFN-ARHGEF12-17E4 Rho guanine nucleotide exchange factor (GEF) 12
AFFN-ARHGEF2-11E6 Rho guanine nucleotide exchange factor (GEF) 12
AFFN-BIRC3-10E9 Baculoviral IAP repeat containing 3
AFFN-BIRC3-10F3 Baculoviral IAP repeat containing 3
AFFN-BIRC3-10G6 Baculoviral IAP repeat containing 3
AFFN-BIRC3-10H11 Baculoviral IAP repeat containing 3
AFFN-BIRC3-11G3 Baculoviral IAP repeat containing 3
AFFN-BIRC3-11H11 Baculoviral IAP repeat containing 3
AFFN-BIRC3-12D12 Baculoviral IAP repeat containing 3
AFFN-BIRC3-12F9 Baculoviral IAP repeat containing 3
AFFN-BIRC3-15B3 Baculoviral IAP repeat containing 3
AFFN-BIRC3-16H8 Baculoviral IAP repeat containing 3
AFFN-BIRC3-17G5 Baculoviral IAP repeat containing 3
AFFN-BIRC3-19C4 Baculoviral IAP repeat containing 3
AFFN-BIRC3-1B11 Baculoviral IAP repeat containing 3
AFFN-BIRC3-2D7 Baculoviral IAP repeat containing 3
AFFN-BIRC3-9D1 Baculoviral IAP repeat containing 3
AFFN-BIRC7-11F1 Baculoviral IAP repeat containing 7
AFFN-BIRC7-11H5 Baculoviral IAP repeat containing 7
AFFN-BIRC7-2B3 Baculoviral IAP repeat containing 7
AFFN-BIRC7-3B3 Baculoviral IAP repeat containing 7
AFFN-BLK-10F9 B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
AFFN-BLK-11H2 B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
AFFN-BLK-14B8 B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
AFFN-BLK-19H2 B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
AFFN-BLK-20G3 B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
AFFN-BLK-6A5 B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
AFFN-BLK-9E2 B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
AFFN-BMX-10D11 BMX non-receptor tyrosine kinase
AFFN-BMX-11C9 BMX non-receptor tyrosine kinase
AFFN-BMX-11D11 BMX non-receptor tyrosine kinase
AFFN-BMX-15D7 BMX non-receptor tyrosine kinase
AFFN-BMX-18E3 BMX non-receptor tyrosine kinase
AFFN-BMX-8H10 BMX non-receptor tyrosine kinase
AFFN-BRCA1-14C4 Breast cancer 1, early onset
AFFN-BRCA1-1G5 Breast cancer type 1 susceptibility protein
AFFN-BRDT-12B2 Bromodomain, testis-specific
AFFN-BRDT-13E3 Bromodomain, testis-specific
AFFN-BRDT-19H3 Bromodomain, testis-specific
AFFN-BTK-8A6 Bruton agammaglobulinemia tyrosine kinase
AFFN-BTK-9A11 Bruton agammaglobulinemia tyrosine kinase
AFFN-BTK-9F2 Bruton agammaglobulinemia tyrosine kinase
AFFN-CAMKK2-10H2 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-1H3 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-2B4 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-3B11 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-3B4 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4E6 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4G8 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4G8-B6 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4G8-E4 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4G8-G7 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4G8-G8 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4G8-H11 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-4G8-H8 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-5D6 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-7E1 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-7E7 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-7E7-D11 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-7E7-E12 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CAMKK2-8B4 calcium/calmodulin-dependent protein kinase kinase 2, beta
AFFN-CBL-1G11 Cbl proto-oncogene, E3 ubiquitin protein ligase
AFFN-CDC34-10D1 Cell division cycle 34
AFFN-CDC34-1G12 Cell division cycle 34
AFFN-CEP170-20B9 Centrosomal protein 170kDa
AFFN-CEP170-7A12 Centrosomal protein 170kDa
AFFN-CHEK2-17D2 Serine/threonine-protein kinase Chk2; Checkpoint kinase 2
AFFN-CIT-1F12 Citron Rho-interacting kinase
AFFN-CIT-1G6 Citron Rho-interacting kinase
AFFN-CIT-2A11 Citron Rho-interacting kinase
AFFN-CIT-2D10 Citron Rho-interacting kinase
AFFN-CIT-3H6 Citron Rho-interacting kinase
AFFN-CSNK1E-13D7 Casein kinase I isoform epsilon
AFFN-CSNK2A1-5F1 Casein kinase II subunit alpha
AFFN-CSNK2A2-5F2 Casein kinase II subunit alpha prime
AFFN-DLG1-4D6 Discs, large homolog 1 (drosophila)
AFFN-DLG2-13F7 Discs, large homolog 2 (drosophila)
AFFN-DLG2-15D2 Discs, large homolog 2 (drosophila)
AFFN-DLG2-17C6 Discs, large homolog 2 (drosophila)
AFFN-DLG2-17F1 Discs, large homolog 2 (drosophila)
AFFN-DLG2-1B9 Discs, large homolog 2 (drosophila)
AFFN-DLG2-1H12 Discs, large homolog 2 (drosophila)
AFFN-DLG2-3A3 Discs, large homolog 2 (drosophila)
AFFN-DLG2-4C3 Discs, large homolog 2 (drosophila)
AFFN-DNTT-13A10 DNA nucleotidylexotransferase
AFFN-DNTT-19B6 DNA nucleotidylexotransferase
AFFN-DNTT-3D7 DNA nucleotidylexotransferase
AFFN-DUSP7-14G9 Dual specificity phosphatase 7
AFFN-ECHS1-5F7 Enoyl CoA hydratase, short chain, 1, mitochondrial
AFFN-ECHS1-7E6 Enoyl CoA hydratase, short chain, 1, mitochondrial
AFFN-ECHS1-7G6 Enoyl CoA hydratase, short chain, 1, mitochondrial
AFFN-ECHS1-9B3 Enoyl CoA hydratase, short chain, 1, mitochondrial
AFFN-ECHS1-9E6 Enoyl CoA hydratase, short chain, 1, mitochondrial
AFFN-ECHS1-9E9 Enoyl CoA hydratase, short chain, 1, mitochondrial
AFFN-EEF2K-10E8 Eukaryotic elongation factor-2 kinase
AFFN-EEF2K-13D2 Eukaryotic elongation factor-2 kinase
AFFN-EEF2K-3E10 Eukaryotic elongation factor-2 kinase
AFFN-EEF2K-3F6 Eukaryotic elongation factor-2 kinase
AFFN-FASN-10H6 Fatty acid synthase
AFFN-FASN-18A8 Fatty acid synthase
AFFN-FASN-19C3 Fatty acid synthase
AFFN-FASN-3E7 Fatty acid synthase
AFFN-FASN-4A1 Fatty acid synthase
AFFN-FASN-4H3 Fatty acid synthase
AFFN-FASN-5H12 Fatty acid synthase
AFFN-FASN-5H9 Fatty acid synthase
AFFN-FASN-6E5 Fatty acid synthase
AFFN-FASN-7A8 Fatty acid synthase
AFFN-FASN-9H3 Fatty acid synthase
AFFN-FER-18A7 Fer tyrosine kinase
AFFN-FER-2G12 Fer tyrosine kinase
AFFN-FER-3D4 Fer tyrosine kinase
AFFN-FER-5F12 Fer tyrosine kinase
AFFN-FER-7F12 Fer tyrosine kinase
AFFN-FES-2F3 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-3B12 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-3D1 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-4D12 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-4G1 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-7B3 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-7C2 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-7G6 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-8D1 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-8D1-B2 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-8D1-B6 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FES-9D2 Tyrosine-protein kinase Fes/Feline sarcoma oncogene
AFFN-FGR-14A10 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-14A3 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-15A5 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-19G5 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-1A7 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-1D12 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-1G12 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-4E7 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-7A2 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FGR-7G3 Feline Gardner-Rasheed sarcoma viral oncogene homolog
AFFN-FH-1A7 Fumarate hydratase, mitochondrial
AFFN-FH-1F6 Fumarate hydratase, mitochondrial
AFFN-FH-2G8 Fumarate hydratase, mitochondrial
AFFN-FUS-11E11 Fused in sarcomas/RNA-binding protein FUS
AFFN-FUS-13B6 Fused in sarcomas/RNA-binding protein FUS
AFFN-FUS-15H5 Fused in sarcomas/RNA-binding protein FUS
AFFN-FUS-16F1 Fused in sarcomas/RNA-binding protein FUS
AFFN-FUS-18B9 Fused in sarcomas/RNA-binding protein FUS
AFFN-FUS-19B2 Fused in sarcomas/RNA-binding protein FUS
AFFN-FUS-5A9 Fused in sarcomas/RNA-binding protein FUS
AFFN-FUS-6F2 Fused in sarcomas/RNA-binding protein FUS
AFFN-FYN-13B9 Tyrosine-protein kinase Fyn/ FYN oncogene related to SRC, FGR, YES
AFFN-FYN-18G7 Tyrosine-protein kinase Fyn/ FYN oncogene related to SRC, FGR, YES
AFFN-FYN-7H11 Tyrosine-protein kinase Fyn/ FYN oncogene related to SRC, FGR, YES
AFFN-GNG2-11F6 Guanine nucleotide binding protein (G protein), gamma 2
AFFN-GNG2-20G6 Guanine nucleotide binding protein (G protein), gamma 2
AFFN-GNG2-2B12 Guanine nucleotide binding protein (G protein), gamma 2
AFFN-GNG2-3B2 Guanine nucleotide binding protein (G protein), gamma 2
AFFN-GOT2-12F6 Glutamic-oxaloacetic transaminase 2, mitochondrial
AFFN-GOT2-15C9 Glutamic-oxaloacetic transaminase 2, mitochondrial
AFFN-GOT2-1A8 Glutamic-oxaloacetic transaminase 2, mitochondrial
AFFN-GOT2-2F2 Glutamic-oxaloacetic transaminase 2, mitochondrial
AFFN-GOT2-5G7 Glutamic-oxaloacetic transaminase 2, mitochondrial
AFFN-GOT2-6B2 Glutamic-oxaloacetic transaminase 2, mitochondrial
AFFN-GOT2-7H1 Glutamic-oxaloacetic transaminase 2, mitochondrial
AFFN-GRB7-1C7 Growth factor receptor-bound protein 7
AFFN-GRB7-1H4 Growth factor receptor-bound protein 7
AFFN-GRIP1-18D11 Glutamate receptor interacting protein 1
AFFN-GRIP1-20E9 Glutamate receptor interacting protein 1
AFFN-GRIP1-9G1 Glutamate receptor interacting protein 1
AFFN-GRK5-10A12 G protein-coupled receptor kinase 5
AFFN-GRK5-17D4 G protein-coupled receptor kinase 5
AFFN-GRK5-18F6 G protein-coupled receptor kinase 5
AFFN-GRK5-2D8 G protein-coupled receptor kinase 5
AFFN-GRK5-3F12 G protein-coupled receptor kinase 5
AFFN-HSD17B10-1B4 Hydroxysteroid (17-beta) dehydrogenase 10
AFFN-HSD17B10-1C2 Hydroxysteroid (17-beta) dehydrogenase 10
AFFN-HSD17B10-1C9 Hydroxysteroid (17-beta) dehydrogenase 10
AFFN-HSD17B10-1H2 Hydroxysteroid (17-beta) dehydrogenase 10
AFFN-HSD17B10-3C9 Hydroxysteroid (17-beta) dehydrogenase 10
AFFN-HSD17B10-4D9 Hydroxysteroid (17-beta) dehydrogenase 10
AFFN-HSH2D-6G7 Hematopoietic SH2 domain containing
AFFN-HSH2D-7B7 Hematopoietic SH2 domain containing
AFFN-HSH2D-8D9 Hematopoietic SH2 domain containing
AFFN-HSH2D-8E8 Hematopoietic SH2 domain containing
AFFN-HSH2D-8F2 Hematopoietic SH2 domain containing
AFFN-HSH2D-9E3 Hematopoietic SH2 domain containing
AFFN-HSPB8-13B6 Heat shock 22kDa protein 8
AFFN-HSPB8-16F8 Heat shock 22kDa protein 8
AFFN-HSPB8-2E10 Heat shock 22kDa protein 8
AFFN-HSPB8-4D5 Heat shock 22kDa protein 8
AFFN-HSPB8-7C5 Heat shock 22kDa protein 8
AFFN-IGFBP2-10B4 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-1B4 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-1H12 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-5D1 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-5F5 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-6D11 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-7G8 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-8G8 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-9A6 Insulin-like growth factor binding protein 2
AFFN-IGFBP2-9D9 Insulin-like growth factor binding protein 2
AFFN-ILK-7C7 Integrin-linked protein kinase
AFFN-INADL-1-15D1 InaD-like protein
AFFN-INADL-1-3G6 InaD-like protein
AFFN-INADL-1-4A11 InaD-like protein
AFFN-INADL-1-5E7 InaD-like protein
AFFN-INADL-1-5H2 InaD-like protein
AFFN-ITK-12A9 IL2-inducible T-cell tyrosine-protein kinase
AFFN-ITK-12B1 IL2-inducible T-cell tyrosine-protein kinase
AFFN-ITK-12F4 IL2-inducible T-cell tyrosine-protein kinase
AFFN-ITK-14G9 IL2-inducible T-cell tyrosine-protein kinase
AFFN-ITK-14H5 IL2-inducible T-cell tyrosine-protein kinase
AFFN-ITK-16C12 IL2-inducible T-cell tyrosine-protein kinase
AFFN-ITK-18H8 IL2-inducible T-cell tyrosine-protein kinase
AFFN-ITK-3A8 IL2-inducible T-cell tyrosine-protein kinase

Antigen List

14-3-3 sigma
26S proteasome non-ATPase regulatory subunit 4
2F7
30S ribosomal protein S3
5-bromo-2′-deoxyuridine BrdU
6XHis peptide, linear
8-oxoguanine DNA glycosylase
A6 Antigen in Biliary Epithelial & Oval cells
Abdominal-B homeobox protein
ABP2 olfactory binding protein
Abrupt
acetylcholine nicotinic receptors, muscle
acetylcholinesterase
Achaete protein
acinar, exocrine gland
Acj6
actin
actin associated antigen, migration-related
actin binding protein 34 (ABP34)
actinin, alpha-
actinin, smooth muscle alpha
Actinomyces naeslundii and oris
Actinomyces naeslundii, oris and israelii
Actinomyces oris
Activating transcription factor 7; ATF7
addressin (PNAd)
adducin-related protein
adenovirus type 5 hexon (human)
ADP-ribosylation factor-like protein 8
Aggregatibacter actinomycetemcomitans
Aggregatibacter actinomycetemcomitans serotype a
Aggregatibacter actinomycetemcomitans serotype a‰
Aggregatibacter actinomycetemcomitans serotype b
Aggregatibacter actinomycetemcomitans serotype c
Aggregatibacter actinomycetemcomitans serotype d
Aggregatibacter actinomycetemcomitans serotype e
Aggregatibacter actinomycetemcomitansserotype d
agrin
Aldo-keto Reductase Family 1 Member B1
Aldo-keto Reductase Family 1 Member C1
Aldo-keto reductase family 1 member C2
alkaline phosphatase isoenzyme
alkaline phosphatase, bone and liver
allatostatin (Ast7)
alpha sarcoglycan
alpha2bBeta3
alpha-2-macroglobulin receptor
alpha-L-fucosidase
aminopeptidase N
ANAPC2; Anaphase promoting complex subunit 2
Anaphase promoting complex subunit 2
angiotensin converting enzyme
Ankyrin repeat and BTB (POZ) domain containing 1
Ankyrin repeat and KH domain containing 1
Ankyrin repeat and zinc finger domain containing 1
Annexin A1 (Annexin I)
Annexin A1 Peptide 1
Annexin A4 Peptide 1
annexin I
annexins I and II
Antennapedia protein
Anti-silencing function 1A histone chaperone
AP-2 alpha
AP-3 (delta subunit)
APA-2 amino acids 618-925
APEX Nuclease I
apoptotic marker in phagocytic cells (nematode)
Aprataxin and PNKP like factor
argos-gene product
ARID3A; AT rich interactive domain 3A (BRIGHT-like)
Armadillo Drosophila protein
Aryl hydrocarbon receptor nuclear translocator-like protein 1
Aspergillus flavus isolate 93803
ASPL-TFE3 type 1
ASPL-TFE3 type 2
AT rich interactive domain 2 (ARID, RFX-like)
AT-hook-containing transcription factor
Atox1
ATPase family AAA domaining containg 2
ATPase family, AAA domain containing 2
ATPase family, AAA domain containing 2; ATAD2
ATPase, (Na (+) K(+)) alpha subunit
ATPase, (Na(+) K(+)) alpha-1 subunit
ATPase, (Na(+) K(+)) alpha-1 subunit (avian)
ATPase, (Na(+) K(+)) beta-1 subunit (avian)
ATPase, (Na(+) K(+)) beta-subunit
ATPase, Ca(+2) fast twitch SR (avian) / SERCA1
ATPase, Ca(+2) fast twitch SR / SERCA1
ATPase, Ca(+2) slow twitch/cardiac SR (avian), SERCA2
ATRX; Alpha thalassemia/mental retardation syndrome X-linked
autoimmune double stranded DNA
autoimmune single stranded DNA
avian myoblastosis virus, p19^(gag)
AVP
axonal filaments, 56 & 58 kDa (amphibian)
axons, CNS (Drosophila)
B lymphoid tyrosine kinase (Tyrosine-protein kinase Blk)
BACH1
BACH2; BTB and CNC homology 1, basic leucine zipper transcription factor 2
Baculoviral IAP repeat containing 3
Baculoviral IAP repeat containing 7
basement membrane marker
Basic helix-loop-helix family, member a9
Basic leucine zipper transcription factor ATF-like 3
Basic leucine zipper transcription factor, ATF-like 2
Basic leucine zipper transcription factor, ATF-like 3
BATF; Basic leucine zipper transcription factor, ATF-like
B-cell CLL/lymphoma 6
B-cell CLL/lymphoma 6; B-cell lymphoma 6 protein
B-cell lymphoma/leukemia 11A
BCL2 like 1
BCL2-like 2
BEAF
Beta Catenin like protein 1
beta-defensin 3
beta-galactosidase
BHK cells overexpressing mouse Glucagon-like peptide 1 receptor
Bicaudal-D
blastema, regenerating
blastemal regeneration cell marker of the newt
BMI1 polycomb ring finger oncogene; Polycomb complex protein BMI-1
BMX non-receptor tyrosine kinase
Bobby sox homolog
bodywall muscle cells
BolA family member 3
BolA-like protein 2
bone sialoprotein II
Botrytis cinerea
brain-derived neurotrophic factor, fish & human
brain-derived neurotrophic factor, mouse
BRCA1 Interacting Protein C-Terminal Helicase 1 Peptide 1
BRD1; Bromodomain containing 1
Breast cancer 1, early onset
Breast Cancer 1, Early Onset Peptide 1
Breast cancer type 1 susceptibility protein
Broad (core)
Broad (Z1)
Broad (Z3)
Bromodomain and PHD finger containing, 1
Bromodomain and WD repeat domain containing 1
Bromodomain containing 1
Bromodomain containing 3
Bromodomain containing 9
Bromodomain, testis-specific
Bruchpilot
Bruton agammaglobulinemia tyrosine kinase
BSX; Brain-specific homeobox
BTB and CNC homology 1, basic leucine zipper transcription factor 2
BTN1A1
BUB3-interacting and GLEBS motif-containing protein ZNF207
cactus
cadherin, B-
cadherin, C-
cadherin, DE-
cadherin, DN-
Cadherin, E-
cadherin, E- (canine)
cadherin, N-
cadherin, R-
cadherin-6B
cadherin-7
cadherin-8
calbindin-32, drosophila
Calcineurin B homologous protein 2 (Hepatocellular carcinoma-associated antigen 520)
calcium/calmodulin-dependent protein kinase kinase 2, beta
Calcyclin (Prolactin Receptor Associated Protein)
calmodulin
Calnexin
Calreticulin Peptide 1
calreticulin, recombinant Dictyostelium
CAMP responsive element binding protein 1
cAMP responsive element binding protein 5
CAMP responsive element binding protein-like 2
cAMP-specific phosphodieserase PDE4A4
cAMP-specific phosphodieserase PDE4A8
cAMP-specific phosphodieserase PDE4D5
Campylobacter rectus
Cap32/34
capping protein alpha-1 & alpha-2 subunits
capping protein beta-1 subunit
capping protein beta-2 subunit
carbohydrate epitope, probably globoseries
Carbonic anhydrase VIII
cardioactive peptide B
CARO2
Casein kinase I isoform epsilon
Casein kinase II subunit alpha
Casein kinase II subunit alpha prime
CASP8AP2; CASP8-associated protein 2
Caspase 8 associated protein 2
catenin, alpha- (Drosophila)
catenin, alpha N
catenin, beta-
catenin, p120
Caudal type homeobox 2
caveolin
CBFB; Core-binding factor subunit beta
Cbl proto-oncogene, E3 ubiquitin protein ligase
Cbl-L protein exon 6 (aa 449-878 of L isoform)
CBX2; Chromobox protein homolog 2
CCAAT/enhancer binding protein (C/EBP), beta
CD1
CD11a (LFA-1 alpha subunit)
CD11a (LFA-1 alpha subunit) (human)
CD11a (LFA-1 alpha subunit), murine
CD11b (Mac-1 alpha subunit), murine
CD11b (Mac-1), murine
CD11b (Mac-1, CR3) (human)
CD133/ Prominin-1
CD18 (beta subunit of CD11, a, b, c), murine
CD18 (beta subunit of CD11a, b, c)
CD2 (LFA-2)
CD21
Cd248
CD31 (PECAM-1)
CD44
CD44 (CRIII)
CD44 human, hyaluronate receptor
CD44 molecule (Indian blood group) Peptide 1
CD45 (lymphocyte common antigen) (human)
CD48
CD58 (LFA-3)
CD63 (human) LAMP
CD64
CD9
CDC5L; Cell division cycle 5-like
Cdk7, recombinant
CEBPE; CCAAT/enhancer binding protein (C/EBP), epsilon
CEBPZ; CCAAT/enhancer binding protein (C/EBP), zeta
Cell cycle and apoptosis regulator 2
Cell division cycle 34
Cell division cycle 34 homolog (S. Cerevisiae)
cell-junction marker
Centrosomal protein 170kDa
chaoptin
Checkpoint kinase 2
chemokine (C-X-C motif) ligand 9
chicken cell marker
Chloride channel calcium activated 3A1; CLCA1 protein
Chloride Intracellular Channel 1
choline acetyltransferase
Choline Kinase Alpha
chondroitin sulfate proteoglycans (carbohydrate epitope)
Chorionic Gonadotropin, beta polypeptide Peptide 1
Chromobox homolog 1
Chromobox homolog 3
Chromobox homolog 5
Chromogranin A
chromosome 1, 55-73 kDa polypeptides
chromosome 11, 40 and 80 kDa polypeptides
chromosome 12, 21 kDa product
chromosome 19, OKa blood antigen / CD147
Citron Rho-interacting kinase
Cleavage stimulation factor subunit 2
Cleavage stimulation factor subunit 2 tau variant
Clec4f
c-MYC
CNS, leech
CNS-specific antigen
Coactosin p17
Coiled-coil and C2 domain containing 1A
collagen (pro-) type I (aminopropeptide)
collagen type II
collagen type III
collagen type IV
collagen type IX
collagen type VI
collagen type X
collagen type XII
collagen type XVIII
collagen(pro-) type I
collagenase
Connectin C1.427
connexin 32
COPS3; COP9 signalosome subunit 3
Coracle
Core-binding factor subunit beta
Core-binding factor, beta subunit
coronin
Coronin N-terminal
Cortexillin I
Cortexillin II
Costal-2 (Cos2)
creatine kinase
Creatine kinase B chain
CREB3L4; CAMP responsive element binding protein 3-like 4
CrebA transcription factor
CREBL2; cAMP responsive element binding protein-like 2
Crumbs Drosophila protein
crystal protein
Crystallin Alpha B
csA (contact site A glycoprotein)
Csp
CSP2 chemosensory protein
CTBP1; C-terminal binding protein 1
C-terminal binding protein 1
C-terminal binding protein 2
Cubitus interruptus (Ci) full length
CUGBP, Elav-like family member 2
CUGBP, Elav-like family member 4
Cut homeobox
Cutoff protein, CG13190, full length protein
CXXC1; CXXC finger protein 1
Cyclic AMP-dependent transcription factor ATF-2
cyclic nucleotide-gated channel (rOCN2, rat)
Cyclin A
cyclin B
Cyclin D binding myb-like Transcription Factors 1
cyp-33E1, recombinant
Cystatin A
Cystatin B
cysteine string protein (CSP), Drosophila
cytokeratin type II (Xenopus)
D4, zinc and double PHD fingers family 1
Dacapo
Dachshund protein, Drosophila
Dally-like protein (Dlp)
DAO5
DAXX; Death-domain associated protein
DAXX; death-domain associated protein
DBX2; Developing brain homeobox 2
DEAD (Asp-Glu-Ala-Asp) box polypeptide 41
DEAD (Asp-Glu-Ala-Asp) box polypeptide 43
Death-domain associated protein
Decapping mRNA 2
decorin
Deformed epidermal autoregulatory factor 1 homolog
Del-1
Deleted in liver cancer 1
Delta, extracellular domain
desmin
dFMR1
dFMRP
DGCR8 microprocessor complex subunit
DHPR alpha-subunit, skeletal muscle
DHPR beta subunit, skeletal muscle
Dip2
dipeptidylpeptidase IV
Disabled protein
Discoidin I (cAMP binding domain)
discs large (C. elegans)
Discs large (Drosophila)
Discs, large homolog 1 (drosophila)
Discs, large homolog 2 (drosophila)
Disp2 peptide (aa731-750 coupled to KLH)
DLAR
DLX3; Distal-less homeobox 3
DMPK
DNA (cytosine-5-)-methyltransferase 3 alpha
DNA (cytosine-5-)-methyltransferase 3-like
DNA ligase 3
DNA nucleotidylexotransferase
DNA repair protein XRCC1
DNA-binding protein Ikaros
DNA-binding protein inhibitor ID-1
DNA-binding protein inhibitor ID-3
DNA-binding protein RFX2
DNA-binding protein RFX5
DNA-binding protein RFX6
DNA-damage inducible transcript 3
DNA-damage-inducible transcript 3
Dorsal root ganglia homeobox
Dorsal, embryonic polarity protein
Doublesex and mab-3 related transcription factor 2
Doublesex- and mab-3-related transcription factor B1
Doublesex protein DNA binding domain (DBD)
DR1; down-regulator of transcription 1, TBP-binding (negative cofactor 2)
DR1-associated corepressor
DR1-associated protein 1 (negative cofactor 2 alpha)
Draper
Dual specificity phosphatase 7
duct, exocrine gland
DVL2; Dishevelled segment polarity protein 2
DVL3; Dishevelled segment polarity protein 3
DYN-1
Dynein heavy chain
Dystroglycan, alpha
dystroglycan, alpha-
dystroglycan, beta-
dystrophin
dystrophin aa 71-74
dystrophin amino acids 1749-2248
dystrophin amino acids 816-1749
dystrophin amino-acids 1749-2248
dystrophin amino-acids 1749-2248 as TrpE fusion protein
dystrophin amino-acids 816-1749
dystrophin fragment encoded by exons 4-16
dystrophin fragment exons 45-50 aa 2145-2439
dystrophin fragment exons 70-79
E2F transcription factor 8
E3 ubiquitin-protein liase RNF8
E3 ubiquitin-protein ligase NEDD4-like
E3 ubiquitin-protein ligase RING2
E3 ubiquitin-protein ligase SMURF1
E4F transcription factor 1
Early B-cell factor 1
ecdysone receptor (EcR common)
ecdysone receptor (EcR) (common), Manduca sexta
ecdysone receptor (EcR) B1-isoform specific, Manduca sexta
ecdysone receptor (EcR-A)
ecdysone receptor (EcR-B1)
EDF1; Endothelial differentiation-related factor 1
EEA1; Early endosome antigen 1
Eef1b2
Efemp2
egg shell marker for C. elegans embryos
EHMT2; Euchromatic histone-lysine N-methyltransferase 2
elav Drosophila protein
elav Drosophila protein; embryonic lethal abnormal vision
ELF2; E74-like factor 2 (ets domain transcription factor)
ELF3; E74-like factor 3 (ets domain transcription factor, epithelial-specific )
ELK1, member of ETS oncogene family
Embryonal carcinoma cell surface carbohydrate
Emerin (amino acids 11-17)
Emerin (amino acids 112-115 and 150-158)
Emerin (amino acids 112-115)
Emerin (amino acids 152-159)
Emerin (amino acids 221-228)
Emerin (amino acids 69-77)
Emerin (amino acids 7-15)
Emerin (amino acids 89-96)
Enabled
endoglin
endoglin (CD105)
endoplasmic reticulum, rough, glycoprotein
Engrail-1
Engrailed/invected gene products
Enolase superfamily member 1, Mitochondrial
Enoyl CoA hydratase, short chain, 1, mitochondrial
ENS-1; Embryonic Normal Stem Cell
entactin (synaptic)
EP300
EpCAM (murine)
EPH receptor B4
EphB1, EphB2, EphB3
ephrin-B1
epidermal growth factor receptor
epithelial stem cell marker
epithelial surface marker, apical
EPS15, Drosophila
ER81
ERM-1, amino acids 209-563
ESRRA; Estrogen-related receptor alpha
ESRRG; Estrogen-related receptor gamma
estrogen receptor alpha, ligand binding domain (aa 304-554)
Estrogen Receptor Binding Site Associated, Antigen 9
Estrogen-related receptor beta; Steroid hormone receptor ERR2
ETC-related transcription factor ELF-1
Ets variant 6
Ets variant 7
ETV7; Ets variant 7
Eukaryotic elongation factor-2 kinase
Eukaryotic translation initiation factor 2, subunit 1 alpha
Eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa
Eukaryotic translation initiation factor 4A3
Eukaryotic translation initiation factor 4E
Even-skipped protein
Even-skipped protein (Drosophila)
Evx1
Exosome complex exonuclease RRP44
Extra Sex Combs (ESC)
Extradenticle protein (EXDHDcc)
Eyeless protein, linker region
Eyes Absent (Eya) protein
Ezrin (p81)
Fas (TNFRSF6) associated factor 1
fasciclin I (Drosophila)
fasciclin I (grasshopper)
fasciclin II (Drosophila)
fasciclin II (Drosophila, all isoforms)
fasciclin II (grasshopper)
fasciclin II (Manduca sexta)
Fasciclin III (Drosophila)
Fascin
Fatty acid synthase
Fatty acid-binding protein, epidermal
Fatty acid-binding protein, intestinal
FBJ murine osteosarcoma viral oncogene homolog B
Fbln2
Feline Gardner-Rasheed sarcoma viral oncogene homolog
female lethal (2)D
Fer tyrosine kinase
FEZ family zinc finger 2
fibrillin 2-like
fibrinogen
fibronectin
fibronectin (III-14 in Hep2)
fibronectin (III-15)
fibronectin, cell binding domain
filament antigen
Fimbrin
Fimbrin (p67)
Flamingo
FLI1; Fli-1 proto-oncogene, ETS transcription factor
floor plate marker
fluorescein isothiocyanate-conjugated to keyhold limpet hemocyanin
Fly Bag-of-marbles
FMR1
FMRP
Forkhead box A3; Hepatocyte nuclear factor 3-gamma
Forkhead box B2
Forkhead box D3
Forkhead box I1
Forkhead box J2
Forkhead box N1
Forkhead box P4
Forkhead box protein P3
Forkhead box protein P4
FosB; FBJ murine osteosarcoma viral oncogene homolog B
FOS-like antigen 2
Fos-related antigen 1
FOXI1; Forkhead box I1
FOXL1; Forkhead box L1
FOXM1; Forkhead box M1
FOXO3; Forkhead box O3
FOXR1; Forkhead box R1
Frizzled protein
Frizzled2
Fstl3
Fukutin
Fumarate hydratase, mitochondrial
Fused (Fu)
Fused in sarcomas/RNA-binding protein FUS
futsch
FXR2
G protein-coupled receptor kinase 5
GA binding protein transcription factor, beta subunit 1
GA-binding protein alpha chain
ganglioside GD1a
ganglioside GD1b
ganglioside GM1
Ganglioside GT1b
GASP (Gene Analogous to Small Peritrophins)
GATA4; GATA binding protein 4
GBX-1 homeobox protein
GBX1; Gastrulation brain homeobox 1
GD2 glycolipid
Gelsolin
gemin4
gemin5
gemin6
Geminin
General transcription factor IIF subunit 2
General transcription factor IIH subunit 2
General transcription factor II-I repeat domain-containing protein 2A
General transcription factors IIi
germ cells, male, rodent
germ-line-specific P granules
gigas gene product
Glass bottom boat; Protein 60A
glass Drosophila protein
GLI family zinc finger 1
Glial cells missing homolog 2
glial precursor
Glorund
Glucagon-like peptide 1 receptor
Glucocorticoid modulatory element-binding protein 2
Glucose phosphate isomerase
Glutamate receptor interacting protein 1
Glutamate receptor subunit, DGluR-IIA
Glutamate-Cysteine Ligase Regulatory Subunit
Glutamic acid decarboxylase; GAD
Glutamic-oxaloacetic transaminase 2, mitochondrial
Glutathione S Transferase Mu3
Glutathione S-Transferase Mu1
Glutathione S-Transferase Mu2
Glutathione S-Transferase Pi 1 Peptide 1
glutathione-S-transferase
Glyceraldehyde-3-phosphate dehydrogenase (hGAPDH)
glycolipid; epitope is an alpha-galactose lactoseries carbohydrate
glycoprotein, Cladosporium herbarum race 4
glycoprotein, Ulocladium
glyoxylate cycle protein
GOBP1 olfactory binding protein
GOBP2 olfactory binding protein
Golgi microtubule-associated protein
Golgin-245 ortholog
gp135/podocalyxin
gp210
GPIb; von Willebrand factor receptor; GPIb/IX complex
Grainyhead-like 1
Grainyhead-like 1 homolog
Grainyhead-like protein 1
GRAM domain containing 4
Green fluorescent protein (GFP)
Green fluorescent protein (GFP) variant
Groucho protein
Growth Factor Receptor-Bound Protein 2 Peptide 1
Growth factor receptor-bound protein 7
GST fused to a fragment of the Klarsicht alpha protein (amino acids 1895-2262) from Drosophila melanogaster
GST fused to a fragment of the Klarsicht alpha protein (amino acids 277-556) from Drosophila melanogaster
GST fused to a fragment of the Klarsicht alpha protein (amino acids 875-1169) from Drosophila melanogaster
GTF2F2; General transcription factor IIF, polypeptide 2, 30kDa
GTF2H2 family member C
Guanine nucleotide binding protein (G protein), gamma 2
Gurken protein
H6 family homeobox 3
Hairy/ enhancer-of-split related with YRPW notif protein
Hairy/ enhancer-of-split related with YRPW notif protein 2
Half pint protein, C-terminal half (amino acids 277-637)
HAND2; Heart and neural crest derivatives expressed 2
HCP4
HCS-1 (Hair Cell Soma-1) / otoferlin
Headcase protein (amino acids 1-417)
Heart and neural crest derivatives expressed 1
Heat shock 22kDa protein 8
Heat shock 27kDa protein 1
Heat Shock 27kDa Protein 1 Peptide 1
Heat Shock 27kDa Protein 1 Peptide 3
Heat shock 60kDa protein 1 (chaperonin)
Heat Shock Protein-100
Heat shock transcription factor 2
Heat shock transcription factors 2
hemapoietic stem cell protein, 74 kDa
Hematopoietic SH2 domain containing
hemocytes, moth larvae
heparan sulfate proteoglycan
heparan sulfate proteoglycan (basement membrane)
Hepatocyte nuclear factor 3-beta
Hepatocyte nuclear factor 4, alpha
Hepatoma derived growth factor-like 1
Hepatoma-derived growth factor
Hepatoma-derived growth factor-related protein 2
HES1; Hes family bHLH transcription factor 1
HES3; Hes family bHLH transcription factor 3
HESX1; HESX homeobox 1
Heterochromatin Protein 1
hevin (SC1, SPARC-like 1)
hexokinase (Type I isozyme)
HHEX; Hematopoietically expressed homeobox
HIF3A; Hypoxia inducible factor 3, alpha subunit
High mobility group 20A
High mobility group box 1
highwire
hindsight: zinc-finger nuclear protein hindsight;
Hisactophilin, Dd gelation factor
histone 2A variant (gamma-H2AV) peptide phosphorylated (QDPQRKGNVILSQAY)
Histone chaperone Anti-silencing function 1B
Histone deacetylase 7
Histone deacetylase 8
Histone H4 Transcription Factors
Histone lysine demethylase PHF8; PHD finger protein 8
Histone-arginine methyltransferase CARM1
Histone-lysine N-methyltransferase EZH2
Histone-lysine N-methyltransferase NSD2
Histone-lysine N-methyltransferase SETD7
Histone-lysine N-methyltransferase SMYD3
HLF; Hepatic leukemia factor
HLFA, beta-subunit
HMGA1; High mobility group AT-hook 1
HMGA1; High mobility group AT-hook 1
HMGB1; High mobility group box 1
HMGXB4; HMG box domain containing 4
HMR-1, amino acids 1099-1223
HNF3b / FoxA2
HNK-1 epitope
Homeobox and leucine zipper encoding
Homeobox and leucine zipper protein Homez
Homeobox B2; HOXB2
Homeobox B6
Homeobox C8
Homeobox protein HMX3
Homeobox protein Hox- B5
Homeobox protein Meis 2
Homeobox protein Meis 3
Homeobox protein Nkx-2.5
Homeobox protein Nkx-3.2
Homeobox protein Nkx-6.1; Nkx6.1
Homeobox protein PKNOX2
Homeodomain-only protein
HOP homeobox
Hoxb4
Hoxc10
Hoxc9
HOXD9; Homeobox D9
HSF1; Heat shock transcription factor 1
HSF5; Heat shock transcription factor family member 5
HSP-60, amino acids 1-547
htsRC
huntingtin
Hydroxysteroid (17-beta) dehydrogenase 10
hypodermal marker
hypodermis (seam cells)
Ia antigen (chicken)
Ia antigen (quail)
ICAM-1
ID2; Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein
ID3; Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein
ID4; Inhibitor of DNA binding 4, dominant negative helix-loop-helix protein
ID4; Inhibitor of DNA binding 4, dominant negative HLH protein
IL2-inducible T-cell tyrosine-protein kinase
InaD-like protein
Indoleamine-pyrrole 2,3 dioxygenase
Inhibitor of growth family, member 1
Inhibitor of growth family, member 4
INSM1; Insulinoma-associated 1
insulin (pro-) non-processed
insulin (proinsulin; C-peptide)
Insulin gene enhancer protein ISL-1
Insulin-like growth factor binding protein 2
integrin alpha 2 (CD49b, VLA2, ITGA2, ECMR II)
integrin alpha V subunit (CD51, fibronectin receptor alpha subunit)
integrin alpha V/5 + beta 5 (CD49e, CD51, fibronectin/vitronectin receptor)
integrin alpha-2
integrin alpha-2 (CD49b)
integrin alpha-2; alpha2beta1 integrin complex
integrin alpha-2b beta-3
integrin alpha-3
integrin alpha-3 (CD49c)
integrin alpha-4 (CD49d)
integrin alpha-5
integrin alpha-5 (avian)
integrin alpha-5 (CD49e)
integrin alpha-6
integrin alpha-6 (avian)
integrin alpha-7 (avian)
integrin alphaPS1 (multiple edematous wing)
integrin alphaPS2 (inflated)
integrin beta
integrin beta 3 (amino acids 26-40)
integrin beta-1
integrin beta-1 (avian)
integrin beta-1 (CD29)
integrin beta-1 (Xenopus)
integrin beta-2 (CD18)
integrin beta-3
integrin betaPS (myospheroid)
integrin, alpha-V beta-5 heterodimer
Integrin, beta-1 subunit
Integrin-linked protein kinase
intercostal nerves
intercostal nerves in a rostrocaudal gradient
Interferon regulatory factor 3
Interferon regulatory factor 8
Interferon-inducible double stranded RNA dependent protein kinase activator A
Interleukin 18
Interleukin 18 Peptide 1
Interleukin 6
intermediate filament subunit
Intestine-specific
Intraflagellar transport protein p139
Intraflagellar transport protein p172
Intraflagellar transport protein p57/55
Intraflagellar transport protein p81
IRF2; Interferon regulatory factor 2
IRF3; Interferon regulatory factor 3
Iroquois-class homeodomain protein IRX-5IRX5
ISL1; ISL LIM homeobox 1
Islet delta cells
Islet-1 homeobox
Islet-1 Islet-2 homeobox
Islet-1 specific homeobox
Islet-2
itchy homolog E3 ubiquitin protein ligase
Jade -1 protein
Jagged1 (JAG1)
JAZF zinc finger 1
JAZF zinc finger 1; JAZF1
JAZF1; JAZF zinc finger 1
Junctions, epidermal cell:cell
JUP; Junction plakoglobin
KDM1A; Lysine (K)-specific demethylase 1A
KDM8; Lysine (K)-specific demethylase 8
kel 1B
Kelch Domain Containing 8A Peptide 1
keratan sulfate
keratan sulfate (brain)
keratin type I
Keratin, type I cytoskeletal 19
Keratin, type II cytoskeletal 8; Cytokeratin endoA
keratinocyte, basal, cell attachment antigen (human)
KH domain containing, RNA binding, signal transduction associated 1
KH domain containing, RNA binding, signal transduction associated 3
KI-67; Marker of proliferation Ki-67
KIAA1967
kinesin
Kinesin family member 13B
Kinesin-like protein KIF2C
Kinetochore protein NDC80 homolog
KLF10; Kruppel-like factor 10
KLF10; Kruppel-like factor 10
KLF15; Kruppel-like factor 15
KLF16; Kruppel-like factor 16
KLOTHO
Krueppel-like factor 15
Kruppel-like factor 1 (erythroid)
Kruppel-like factor 10
Kruppel-like factor 14
Kruppel-like factor 17
Kruppel-like factor 5 (intestinal)
Kruppel-like factor 7
L1 protein (rat)
L1CAM and NCAM
L1-like CAM (avian)
L3MBTL4; L(3)mbt-like 4 (Drosophila)
lactadherin
lactase-phlorizin hydrolase
Lactoylglutathione lyase
lacunin
lamin
lamin A/C (recombinant)
lamin C
lamin Dm0
laminin
laminin 5 (epiligrin, LAMA3, laminin-5 alpha subunit)
laminin B2
laminin, gamma-1 chain
laminin, S-
laminin/fibronectin receptor
laminin-binding lectin
LAMP (gene symbol: Lsamp)
LAMP-1
LAMP-1 (CHO)
LAMP1; Lysosome-associated membrane glycoprotein 1
LAMP-2
LAMP-2 (110 kDa lysosomal membrane glycoprotein)
LAMP-2 (CHO)
LAMP-2 (human)
late bloomer
L-CAM, E-cadherin, uvomorulin
LCOR; Ligand-dependent nuclear receptor corepressor
LET-413 (amino acids 460-606)
Lethal(3)malignant brain tumor-like protein 4
Leucine aminopeptidase
Leucine rich repeat (in FLII) interacting protein 1
leukocyte, activated, cell surface glycoprotein
LEUTX; Leucine twenty homeobox
Ligand-dependent nuclear receptor corepressor-like
Lim 1+2 / LhxV5
LIM domain binding 1
LIM homeobox 2; LHX2
LIM homeobox 4
LIM/homeobox protein Lhx2
Lim3
LIN-28 homolog A
Lin-7 homolog C
link protein
lipooligosaccharide (LOS)
LMP-1, amino acids 18-160
LMX
L-myc protein
lost protein, recombinant, expressed in E. coli
lozenge
Lymphoid-specific helicase,
Lysine (K)-specific demethylase 2A
Lysine (K)-specific demethylase 4A
Lysine (K)-specific demethylase 4C
Lysine (K)-specific demethylase 4E
Lysine (K)-specific demethylase 6B
lysine decarboxylase (E. corrodens)
Lysine(K)-specific demethylase 6B
Lysine-specific demethylase 2A
lysosomal membrane glycoprotein (formerly called cv24)
lysosomal membrane glycoprotein (LEP-100) / CD107
Lysosomal-associated membrane protein 1; Lamp-1 ; CD107a
M2, membrane protein
M6, membrane protein
MAFB; V-maf avian musculoaponeurotic fibrosarcoma oncogene homolog B
MAFF; V-maf avian musculoaponeurotic fibrosarcoma oncogene homolog F
MAFG transcription factor
major sperm protein (MSP)
Malate dehydrogenase 1 NAD (soluble)
Malate dehydrogenase 2, NAD (mitochondrial)
maltase-glucoamylase
Maltose binding protein
mannose 6-phosphate / IGF II receptor, cation-independent
mannose 6-phosphate receptor, cation-dependent
MAT2B; Methionine adenosyltransferase II, beta
Math1 (Atoh1)
MAX; MYC associated factor X
MAX-like protein X
MAZ; MYC-associated zinc finger protein (purine-binding transcription factor)
MBNL1 (muscleblind-like splicing regulator 1)
MBNL2 protein (muscleblind-like splicing regulator 2)
MBNL3 protein (muscleblind-like splicing regulator 3)
MBP-sigma 1s
MBP-sigma NS-His
mCherry fluorescent protein
MED4; Mediator complex subunit 4
Mediator complex subunit 1
Mediator of DNA-damage checkpoint 1
Megakaryocyte-associated tyrosine kinase
Meis homeobox 2
Meis homeobox 3
MEIS2; Meis homeobox 2
melanoblasts and melanocytes of neural crest origin (avian) / glutathione S-transferase (alpha subunit)
Melanoma Antigen Family A, 4
Menin
Mesoderm posterior 1 homolog
mesoderm, early, rodent
Metastasin 100 calcium-binding protein A4 (Calvasculin)
Methyl CpG Binding Protein 1
Methyl-CpG binding domain protein 4
METTL21A; Methyltransferase like 21A
MHC class I
MHC class II
Microcephalin
microfibrils (sea urchin)
mineralocorticoid receptor
Mitogen-activated protein kinase 1
Mitogen-activated protein kinase 14
Mitogen-activated protein kinase 8
Mitogen-activated protein kinase kinase kinase 7
Mitotic spindle assembly checkpoint protein MAD2A
MLLT10; Protein AF-10
MLLT3; AF-9
MLX interacting protein
Mmp1 catalytic domain
Mmp1 hemopexin domain
MNR2/HB9/Mnx1
Moesin
Mortality factor 4-like 1
Mothers against decapentaplegic homolog 1
Mothers against decapentaplegic homolog 4
mouse Rb, last 200 amino acids (GST-Rb)
MSH3 aa 24-308
MSX1+2
MUC17 CRD1 L CRD2
Mucin 1, cell surface associated Peptide 1
Mucin 1, cell surface associated Peptide 2
Multiple endocrine neoplasia I
Muscle
muscle fast C-protein
muscle marker
muscle slow C-protein
muscle/neurite marker
Muscleblind-like splicing regulator 3
Mutanase G
MYC induced nuclear antigen
MYCN; N-myc proto-oncogene protein
Myeloid zinc finger 1
MYO1B; Myosin IB
myoblast marker (avian)
myoblast, chondrocyte marker (avian)
myoblast, fibroblast marker (avian)
Myocyte enhancer factor 2A
Myocyte enhancer factor 2B
Myocyte enhancer factor 2C
MyoD
Myogenin
myomesin
myosin (embryonic)
myosin (human neonatal slow and fast IIa fibers)
Myosin all isoforms
myosin fast muscle light chain 2
myosin heavy chain
Myosin heavy chain (all but 2X)
Myosin heavy chain (all fast isoforms)
Myosin heavy chain (human fast fibers)
Myosin heavy chain (human nascent secondary and all fast fibers)
Myosin heavy chain (human neonatal and adult fast fibers)
Myosin heavy chain (human neonatal fast IIa fibers)
Myosin heavy chain (human slow fibers)
Myosin heavy chain (slow and 2A)
Myosin heavy chain (slow, alpha- and beta-)
myosin heavy chain A
Myosin Heavy Chain Type I
Myosin Heavy Chain Type IIA
Myosin Heavy Chain Type IIB
myosin heavy chain, adult
myosin heavy chain, avian fast isoforms and rat, rabbit isoforms including type IIb fibers
myosin heavy chain, avian fast isoforms and rat, rabbit, and turtle isoforms
myosin heavy chain, avian fast isoforms and rat, turtle, newt, frog, fish, ray, and shark isoforms
myosin heavy chain, avian slow isoforms; reacts with isoforms of other species
myosin heavy chain, avian slow myosin and mammalian isoforms
myosin heavy chain, avian slow myosin heavy chain 1, 2 and 3
myosin heavy chain, avian slow myosin heavy chain 2 and 3; slow muscle fibers in zebrafish
myosin heavy chain, embryonic
myosin heavy chain, embryonic and adult fast
myosin heavy chain, embryonic and neonatal fast
myosin heavy chain, fast, 2A
myosin heavy chain, fast, 2B
Myosin heavy chain, fast, 2X
myosin heavy chain, fast, extraocular specific
myosin heavy chain, fast, jaw muscle specific
myosin heavy chain, multiple avian and rat, rabbit, turtle, newt and fish isoforms
myosin heavy chain, neonatal and adult
myosin heavy chain, neonatal fast
myosin heavy chain, sarcomere
myosin heavy chain, slow, SM1 only
myosin heavy chain, slow, SM2
myosin heavy chain, slow, SM2 only
myosin heavy chain, SM2 and atrial
myosin heavy chain, ventricular
myosin II
myosin II heavy chain
myosin IIB, cytoplasmic non-muscle
myosin light chain 1 and 3f (LC1f/3f)
myosin light chain 1s (LC1s)
myosin light chain 1s, 2s, 1f and 2f (LC1s, LC1f, LC2s, LC2f)
myosin, sarcomere (MHC)
myosin-VIIa
myotactin
myotendinous antigen (tenascin)
MZF1; Myeloid zinc finger 1
Na-K-Cl cotransporter
Na-K-Cl cotransporters (shark)
NAPA-73 (neurofilament-associated protein, 73 kDa)
NCAM
NCAM (cytoplasmic domain)
NCAM (extracellular domain)
NCAM (sialylated form); PSA-NCAM
NCAM/L1CAM leech homologue
NCK adaptor protein 1
NCOA1; Nuclear receptor coactivator 1
NEDD8-conjugating enzyme Ubc12
Nervana protein
nervous system
Nestin (intermediate filament protein)
Nestin/radial glial marker
neural associated ganglioside
neural crest cells
neural marker
neural precursor cell expressed, developmentally down-regulated 4 isoform 1
neural precursor cells
neural retinal gangliosides (9-0-acetyl-GD3)
neural specific
neural tube, dorsal
neurocan (C-terminal epitope)
neurocan (N-terminal epitope)
neurocan receptor
neurofilament (160 kDa)
Neurofilament (165 kDa)
Neurofilament associated
neurofilaments
neurofilaments, primary sensory and motor
neurogenin 3
neuroglian (Drosophila, neuron-specific)
neuroglian (Manduca sexta)
Neuromedin-B peptide
neuromuscular junction and reactive Schwann cell associated antigen
neuron (motor) antigen
neuronal cell surface marker
neuronal cell surface marker (SC-1, DM-GRASP, BEN)
neuronal marker (cytoplasmic)
neuronal marker (TAG-1)
neuronal, mesencephalic trigeminal cell surface marker
neuronal, motor, marker (SC-1)
Neurons, cephalic ganglia and ventral cord
neurons, cytoplasmic
neuropil region and primary motor neuron axons
Neuropilin-1
neurotactin (Drosophila)
NFATc1
NFATc2
NFE2L2; Nuclear factor, erythroid 2-like 2
NFKB1; Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1
NFKB2; Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 (p49/p100)
NFYB; Nuclear transcription factor Y, beta
NFYC; Nuclear transcription factor Y, subunit gamma
NHE3, cation proton antiporter 3
nicotinic receptor, neuronal
nidogen/entactin
NINJ2; Ninjurin 2
Nkx2.2 transcription factor
NKX2-5; NK2 homeobox 5
NKX3-1; NK3 homeobox 1
Nkx6.1
N-lysine methyltransferase SETD6
N-lysine methyltransferase SMYD2
N-myc (and STAT) interactor
N-myc proto-oncogene protein
NO66; Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
Non-histone chrmosomal protein HMG-14.
Non-histone chromosomal protein HMG-14
Norovirus RNA-dependent RNA polymerase
Notch, extracellular domain, EGF repeats #12-20
Notch, extracellular domain, EGF repeats #5-7
Notch, intracellular domain
Notch1
Notch2
notochord and neuropil
notochord marker
Nov
NR5A1; Nuclear receptor subfamily 5, group A, member 1
NrCAM
NRF1; Nuclear respiratory factor 1
Nuclear factor 1 A-type
Nuclear factor I A-type
Nuclear factor of activated T-cells, cytoplasmic 3
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2 (p49/p100)
Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 2 Peptide 1
Nuclear factor, interleukin 3 regulated
nuclear lamins II/III (Xenopus)
nuclear membrane marker
Nuclear receptor co-repressor 1
Nuclear receptor subfamily 0, group B, member 1
Nuclear receptor subfamily 1, group D, member 1
Nuclear receptor subfamily 1, group D, member 2
Nuclear receptor subfamily 2, group C, member 1
Nuclear receptor subfamily 5, group A, member 2
Nuclear respiratory factor 1
nucleolar protein
nucleolin (95 kDa and 90 kDa isoforms)
nucleolin (95 kDa isoform)
nucleoplasmin
Nucleoplasmin-3
Nucleoside Diphosphate Kinase A (nm23-H1)
Nucleoside Diphosphate Kinase B
Nucleosome assembly protein 1-like 5
Nucleus accumbens-accociated protein 1
Nucleus accumbens-associated 1
Nucleus accumbens-associated protein 2
Nucleus, intestine and epidermis
nullo-GST fusion protein, an inframe of the entire nullo protein to c-terminus of GST
Numb
OBFC1; Oligonucleotide/oligosaccharide-binding fold containing 1
oligodendrocyte (myelin) marker (amphibian)
oligodendrocytes and their processes
oncomodulin (beta-parvalbumin)
One cut homeobox 2
ONECUT1; One cut homeobox 1
orb protein
orb2 protein
ORC-2
Origin recognition complex, subunit 1
Ornithine Decarboxylase 1
Orthodenticle homeobox 2
Osa
osteonectin
osteopontin
OTU domain, ubiquitin aldehyde binding 1
OTU domain, ubiquitin aldehyde binding 2
OTU domain-containing protein 6B
Otx1
outer membrane protein-19 (OMP-1g)
P granule
P granule + body muscle
P2X7
p46 cell surface protein excluded from macropinocytic cup
p53
P6 protein N-terminus Haemophilus influenzae
P6 surface antigen from Haemophilus influenzae
p80 endosomal membrane protein
P85A
PABA peptide hydrolase (meprin)
Paired box 5
Paired box 9
Paired related homeobox 2
PAR-3
paramyosin
Parvimonas micra
PAS-7
Patched
PAWR; PRKC apoptosis WT1 regulator
Pax3
Pax4 fusion protein (aa 132-171)
PAX5; Paired box 5
Pax6
Pax7
PAX-interacting protein 1
PBP2 olfactory binding protein
PBP3 olfactory binding protein
PBX4; Pre-B-cell leukemia homeobox 4
PBX4; Pre-B-cell leukemia homeobox 4
Pdx1
PDZ and LIM Domain 1
peanut gene protein product
PECAM
Peptide II B 80kD
Peregrin; Bromodomain and PHD finger containing, 1
Pericardin
Perilipin 2
perlecan
perlecan (domain IV)
Peroxiredoxin 2 Peptide 1
Peroxiredoxin 2 Peptide 2
Peroxiredoxin 4
Peroxiredoxin 4 Peptide 1
Peroxisome proliferator-activated receptor alpha
Peroxisome proliferator-activated receptor delta
PGBD1; PiggyBac transposable element derived 1
Pgp-1 (Ly-24) lymphocyte cell adhesion glycoprotein
pharyngeal marker
PHD finger protein 10
PHD finger protein 19
PHD finger protein 21B
PHD finger protein 7
PHD finger protein 8; Histone lysine demethylase PHF8
Phenylethanolamine N-methyltransferase
phosphacan/protein tyrosine phosphatase – z/b
Phosphatidylethanolamine Binding Protein 1
Phosphatidylinositol 3-kinase regulatory subunit alpha
phosphatidylinositol-specific phospholipase C
Phosphogluconate dehydrogenase
Phosphoglycerate dehydrogenase
Phosphoinositide-3-kinase, regulatory subunit 1 (alpha)
Phosphoinositide-3-kinase, regulatory subunit 2 (beta)
Phosphoserine Aminotransferase 1
Phosphoserine phosphatase-like
photoreceptors (rods and cones)
photoreceptors (rods only)
pigment cell marker (sea urchin)
Pigment dispersing factor (PDF) precursor-related peptide
Pigment-dispersing factor neuropeptide
PIKFYVE
PIKFYVE; Phosphoinositide kinase, FYVE finger containing
PLAG1; Pleiomorphic adenoma gene 1
plasmalemma vesicle-associated protein (PLVAP)
plateins (alpha-, beta- & gamma-)
plateins (beta- & gamma-)
PLXNB1; Plexin B1
Podoplanin
POLE3; Polymerase (DNA directed), epsilon 3, accessory subunit
Poly (ADP-ribose) polymerase 1
Poly (ADP-ribose) polymerase family, member 11
Polychaetoid
Polycomb group ring finger 3
Polycomb group ring finger 6
Polymerase (DNA directed), lambda
Polymerase (DNA directed), mu
Pop1 (BVES)
porin
Porphyromonas gingivalis
Porphyromonas gingivalis (cell surface antigen)
Posterior sex combs protein
Potassium channel modulatory factor 1
POU class 5, homeobox 1
POU class 6 homeobox 1
POU3F2; POU class 3 homeobox 2
POU5F1; POU class 5 homeobox 1
PPARD; Peroxisome proliferator-activated receptor delta
PPP1R10; Protein phosphatase 1, regulatory subunit 10
PPP1R10; Serine/threonine-protein phosphatase 1 regulatory subunit 10
PPP5C; Protein phosphatase 5, catalytic subunit
PR domain containing 7; PRDM7
PR domain zinc finger protein 1
PR domain zinc finger protein 13
PR domain zinc finger protein 4
PR domain zinc finger protein 8
PRDM16; PR domain containing 16
PRDM2; PR domain containing 2, with ZNF domain
PRDM7; PR domain containing 7
PRDM7; PR domain containing 7
PRDM8; PR domain zinc finger protein 8
Pre-B-cell leukemia homeobox 1
Prevotella intermedia (cell surface antigen)
Prevotella intermedia and nigrescens (cell surface antigen)
primordial germ cell surface marker (mouse)
PRMT7; Protein arginine methyltransferase 7
profilin
profilin II proteins
Proliferating Cell Nuclear Antigen Peptide 1
Prospero homeobox 1
Prospero protein
Proteasome subunit
Proteasome subunit 5
Protein arginine methyltransferase 6
Protein C-ets-1
Protein L-Myc
Protein Phosphatase 2A
Protein Smaug homolog 2
Protein tyrosine kinase 6
protein tyrosine phosphatase 69D
Protein tyrosine phosphatase, non-receptor type 1
protein tyrosine phosphatase, non-receptor type 6
protein tyrosine phosphatase, receptor-linked, DPTP10D
protein tyrosine phosphatase, receptor-linked, DPTP99A
proteoglycan, hyaluronic acid binding region; aggrecan
Proto-oncogene c-Fos
Proto-oncogene tyrosine-protein kinase Src
PRRX2; Paired related homeobox 2
PTP-ER
Pumilio homolog 1
puromycin
Putative histone-lysine N-methyltransferase PRDM6
Quail cell marker
Quail endothelial cell surface
RAC-gamma serine/threonine-protein kinase
RAD18 Homolog Peptide 1
RAD52 homolog (S. cerevisiae)
radial glial cells
radial glial cells / vimentin
Rarres2
Ras-related C3 botulinum toxin substrate 1 (rho family small GTP binding protein Rac1)
RBBP5; Retinoblastoma binding protein 5
RCOR2; REST corepressor 2
RecD protein
Receptor-type tyrosine-protein phosphatase delta
Receptor-type tyrosine-protein phosphatase epsilon
Receptor-type tyrosine-protein phosphatase-like N
reelin
Reg1a
Reg3g
Regulation of nuclear pre-mRNA domain containing 1A
RelA-associated inhibitor
relaxin hormone
Relish
reovirus
reovirus capsid protein mu 1C
reovirus gamma 2 vertex protein
reovirus outer capsid protein sigma 3
reovirus sigma 1s
reovirus sigma NS
Repo; Reversed polarity protein
REST corepressor 3
Retina and anterior neural fold homeobox
Retinal homeobox protein Rx
retinal space (mechanoreceptors?)
Retinoic acid receptor RXR-gamma
Retinoic acid receptor, beta
Retinoid X receptor RXR- gamma
Retinoid X receptor, gamma
RFX5; DNA-binding protein RFX5
RFX6; Regulatory factor X, 6
RFXANK; Regulatory factor X-associated ankyrin-containing protein
RGCC; Regulator of cell cycle
RGS12 (“Regulator of G Protein Signaling-12”); N-terminal peptide PDZ & PTB domains
Rho guanine nucleotide exchange factor (GEF) 12
rho1
rhoB
rhodopsin 1 (Rh1 Drosophila)
Rhox homeobox family, member 2
Ribonucleotide Reductase M2 Peptide 1
Ribonucleotide Reductase M2 Peptide 2
ribosomal protein L3
Ribosomal protein S6 kinase alpha-5
ribosome, (E. coli)
ribosome, 30S (E. coli)
rim
RME-1, amino acids 333-575
RNA binding protein 8A
Rnase1
RNF113B; Ring finger protein 113B
RNF20; Ring finger protein 20, E3 ubiquitin protein ligase
Robo (Drosophila)
Robo1 (vertebrate)
Robo3 cytoplasmic (Drosophila)
Robo3 extracellular (Drosophila)
Rop
Ror2 (Nt 2535-2835)
RORA; RAR-related orphan receptor A
RORgt
rough Drosophila protein
Rumpelstiltskin
Runt-related transcription factor 2
RUVBL1; RuvB-like AAA ATPase 1
RXRA; Retinoid X receptor, alpha
ryanodine receptor, skeletal
ryanodine receptors
S100 calcium binding protein A2
SAC1
S-adenosylhomocysteine hydrolase
sarcalumenin
SATB1; SATB homeobox 1
SAX7, recombinant amino acids 1051-1144
scabrous Drosophila gene protein
SCAND3; SCAN domain containing 3
SCAR
Schwann cell & myoblast plasma membrane glycoprotein
Schwann cell marker, P(o) (avian)
Schwann cell myelin protein
Scm-like with four mbt domains 1
Scm-like with four MBT domains 2
SCRT1; Scratch family zinc finger 1
Secretory cell, peripharyngeal
selectin, E-
Selenoprotein P
Sema I (grasshopper)
Sema II
sensory cilia and excretory pore marker
Serine/threoinine-protein kianse Chk2
Serine/threonine-protein kinase Chk2; Checkpoint kinase 2
Serine/threonine-protein kinase D1
Serine/threonine-protein kinase OSR1
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin) Member 6 Peptide 1
Serpin Peptidase Inhibitor, Clade A, Member 1
Serrate, RNA effector molecule
SET nuclear proto-oncogene
Seven-up
Sex comb on midleg-like protein 4
Sex combs reduced homeotic protein
Sex determining region Y protein
sex-lethal protein
SH2 domain containing 1A; Duncan disease SH2- protein; SLAM-associated protein
SH2 domain containing 4A
SH2 domain-containing protein 1A
SH2 domain-containing protein 3A
SH2 domain-containing protein 4A
SH2B adaptor protein 2
SH3-domain binding protein 2
Sharpin
SHC (Src homology 2 domain containing) family, member 4
Shot
sialomucin complex (Muc4)
sidestep
Signal transducer and activator of transcription 1, 91kDa
Signal transducer and activator of transcription 1-alpha/beta
Signal transducer and activator of transcription 4
Signal transducer and activator of transcription 5A
Signal transducer and activator of transcription 5B
Sir2 (Drosophila)
SIRT2; Sirtuin 2
Sirtuin 1
Sirtuin 2
Sirtuin 5, mitochondrial
Sirtuin 5;
SIX homeobox 5
SIX5
skeletal muscle marker, 102 kDa
SKI-like protein
SLC25A24; Solute carrier family 25 (mitochondrial carrier; phosphate carrier), member 24
SLC30A9; Zinc transporter 9
SLC4A1, anion exchanger 1
slit protein, C-terminal
Slug
SMAD family member 3
SMAD family member 7
Smad nuclear-interacting protein 1
SMAD4; SMAD family member 4
Small ubiquitin-related modifier (SUMO)
SMARCC2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
SMARCE1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily e, member 1
SMN protein aa 159-209
SMN protein aa 159-209 Exon 4
SMN protein aa 210-241 Exon 5
SMN protein aa 28-91
SMN-interacting protein-1 (Gemin2)
Smoothened (Smo)
Snail family zinc finger 3
snRNA-activating protein complex subunit 4
SNW domain containing 1
Sodium/bile acid cotransporter
Solute Carrier Family 31 (Copper Transporter), Member 1 Peptide 1
Solute Carrier Family 31 (Copper Transporter), Member 2 Peptide 1
somatomedin-C; Sm-C/IGF-1
sonic hedgehog
SOX12; SRY (sex determining region Y)-box 12
SOX3; Transcription factor SOX-3
SOX4; (SRY sex determining region Y)-box 4
SOX4; SRY (sex determining region Y)-box 4
SP110 nuclear body protein
SP140 nuclear body protein
SPARC (osteonectin)
SPARC, recombinant human
Spectrin, alpha
Spermatogenesis and oogenesis specific basic helix-loop-helix 1
Spermidine or Spermine N1-Acetyltransferase 1
Spindle-F full length protein
Spitz, extracellular domain
Spleen tyrosine kinase
Squamous cell carcinoma antigen 1
Squash protein, CG 4711, full length protein
Squid A protein, full length
Squid S protein, full length
SQV-8, amino acids 150-349
Src homology 2 domain containing transforming protein D
SRY (sex determining region Y)-box 13
SRY (sex determining region Y)-box 4
SRY (sex determining region Y)-box 9
SSBP4; Single stranded DNA binding protein 4
SSEA-1/ alpha-(1,3)-fucosyltransferase / CD15
SSEA-3 (carbohydrate from 4-8 cell mouse embryos)
SSEA-4 (carbohydrate from human embryonal carcinoma)
STAM-binding protein
STAT1; Signal transducer and activator of transcription 1, 91kDa
STAT2; Signal transducer and activator of transcription 2, 113kDa
STAT3; Signal transducer and activator of transcription 3
STAT4; Signal transducer and activator of transcription 4
STAT5A; Signal transducer and activator of transcription 5A
STAT5B; Signal transducer and activator of transcription 5B
Steroidogenic factor 1
stromal cell surface marker
sucrase-isomaltase
Sulfotransferase family 1E, estrogen-preferring, member 1 [Homo sapiens]
SUMO aa76-86
SUMO-1
SUMO-2
Suppressor of cytokine signaling 2
Suppressor of fused (Su (fu))
SWI/SNF complex subunit SMARCC1
SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a-like 1
SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1
SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related
SYAP1; Synapse associated protein 1
sympathoadrenal marker
Synapse-associated protein 47 kDa; SAP47
Synapsin
Synaptic vesicle glycoprotein 2A; synaptic vesicles
synaptobrevin
Synaptotagmin
synaptotagmin 1, cytoplasmic domain
synaptotagmin B
synaptotagmin, cytoplasmic domain
Sync
Syntaxin
synuclein, alpha & beta
synuclein, gamma (breast cancer-specific protein 1) Peptide 1
synuclein-gamma
TAC-1
TADA2B; Transcriptional adaptor 2B
talin
talin (avian)
Talin carboxy terminus 534 amino acids
talinA (N-terminal)
Tango
Tannerella forsythia
TAR (HIV-1) RNA binding protein 2
Tau
TAX1BP1; Tax1 (human T-cell leukemia virus type I) binding protein 1
T-box 19
T-box transcription factor TBX19
T-box transcription factor TBX4
TBX19; T-box 19
TBX4; T-box 4
TCF25 Transcription Factors 25 (basic helix-loop-helix)
TEA domain family member 3
Telomeric Repeat Binding Factor 2 Peptide 1
tenascin
Tensin 1
Tensin 3
Tensin 4
TERF2; Telomeric repeat binding factor 2
TERF2IP; Telomeric repeat binding factor 2, interacting protein
tetraspanin large extracellular loop amino acids 111-217
TFAP2D; Transcription factor AP-2 delta
TGFb3, active domain
TGFb3, latent domain
TGIF1; TGFB-induced factor homeobox 1
TGIF2LX; TGFB-induced factor homeobox 2-like, X-linked
THAP domain containing 5
THAP domain containing 9
THAP domain-containing protein 11
THAP domain-containing protein 4
THAP10; THAP domain containing 10
Thyroid hormone receptor, alpha
Thyroid Stimulating Hormone, Beta Peptide 1
Thyroid Stimulating Hormone, beta Peptide 2
Titin
Topoisomerase I
topoisomerase I mitochondrial
TOX high mobility group box family member 3
TOX3; TOX high mobility group box family member 3
TP53; Tumor protein p53
Transcription elongation factor A (SII)-like 8
Transcription facotr RelB
Transcription factor Sp5
Transcription factor 25
Transcription factor AP-2 alpha
Transcription factor AP-2 beta
Transcription factor AP-2 gamma
Transcription factor CP2; Alpha-globin transcription factor CP2
Transcription factor elt-2
Transcription factor ETV6; Ets variant 6
Transcription factor Ovo-like 2
Transcription factor p65 or RELA
Transcription factor RelB
Transcription factor RFX3
Transcription factor SOX-9
Transcription factor Spi-C
Transcription Factors 24
Transcription Factors 25 (basic helix-loop-helix)
Transcription Factors AP-2 alpha (activating enhancer binding protein 2 alpha)
transcription factors E2F 6
transcription factors Ovo-like 2
transcription factors Spi-C
Transcriptional adaptor 3
Transcriptional enhancer factor TEF-3
Transcriptional regulator ERG
Transcriptional repressor NF-X1
transferrin receptor
Transgelin Peptide 1
transglutaminase, tissue
transitin
transketolase
Transthyretin
triadin
Trio
Tripartite motif containing 24
tRNA aspartic acid methyltransferase 1
tropomyosin
tropomyosin, chicken gizzard
tropomyosin, gizzard
tropomyosin, muscle
tropomyosin, recombinant human, isoform 5 and 4 fusion (hTM5/4) protein
tropomyosin, recombinant, isoform 5 and 4 fusion (hTM5/4) protein
troponin I, cardiac
troponin I, skeletal and cardiac
troponin T
troponin T, cardiac
troponin T, skeletal muscle specific
TRP protein (transient receptor potential)
truncated version of sry-a protein which contains amino acids 46 to 530 of sry-a
TSC22 domain family, member 1
TSC22D4; TSC22 domain family, member 4
TSLP
Tubulin
tubulin (alpha-)
tubulin (beta-)
Tubulin, beta
Tudor and KH domain containing
Tumbleweed
Tumor necrosis factor (ligand) superfamily, member 10
Tumor necrosis factor receptor superfamily member 9
Tumor protein p53
Tumor-associated Calcium Signal Transducer 2
tyrosine 3-monooxygenase or tryptophan 5-monooxygenase activation protein, beta polypeptide
tyrosine 3-monooxygenase or tryptophan 5-monooxygenase activation protein, epsilon polypeptide
tyrosine hydroxylase
Tyrosine-protein kinase Fes/Feline sarcoma oncogene
Tyrosine-protein kinase Fyn/ FYN oncogene related to SRC, FGR, YES
Tyrosine-protein ZAP-70
Tyrosyl-DNA Phosphodiesterase 2
Ubiquitin carboxyl-terminal hydrolase 14
Ubiquitin carboxyl-terminal hydrolase 16
Ubiquitin carboxyl-terminal hydrolase isozyme L1
Ubiquitin carboxyl-terminal hydrolase L3 (ubiquitin thiolesterase)
Ubiquitin carboxyl-terminal hydrolase L5
Ubiquitin Conjugating Enzyme E2C Peptide 1
Ubiquitin Conjugating Enzyme E2C Peptide 2
Ubiquitin Conjugating Enzyme E2E2
Ubiquitin Conjugating Enzyme E2L 6
Ubiquitin Conjugating Enzyme E2L 6; UBE2E1
Ubiquitin protein ligase E3A
Ubiquitin specific peptidase 7
Ubiquitin-conjugating enzyme E2 A
Ubiquitin-conjugating enzyme E2 B
Ubiquitin-conjugating enzyme E2 D1
Ubiquitin-conjugating enzyme E2 Q1
ubiquitin-conjugating enzyme E2, J1
Ubiquitin-conjugating enzyme E2C
ubiquitin-conjugating enzyme E2E 1
Ubiquitin-conjugating Enzymes E2B
Ubiquitin-like modifier activating enzyme 1
Ubiquitin-protein ligase E3A
UBQLN2; Ubiquilin 2
Ultrabithorax 5′ exon (107 amino acids)
Ultrabithorax protein
UNC-10, amino acids 1-144
Upstream transcription factor 2, c-fos interacting
Us9 (pseudorabies virus)
USF2; Upstream transcription factor 2, c-fos interacting
utrophin
utrophin aa 113-371
V_H_ATpase c-subunit
vasa
vasa protein
Vav 1 guanine nucleotide exchange factor
Vav 2 guanine nucleotide exchange factor
VCAM
VCAM-1
V-crk avian sarcoma virus CT10 oncogene homolog
VENTX homeobox protein
VENTX; VENT homeobox
VENTX; VENT homeobox
v-erb-b2 erythroblastic leukemia viral oncogene homolog Peptide 1
versican (hyaluronate-binding region)
Villin-like protein quail; 6B9
Vimentin
vimentin (Xenopus)
vimentin; radial and radial glial cell marker
vinculin
vinculin, meta-vinculin
visinin
v-src avian sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog
Wash
Wash cDNA/GST fusion protein
Wasp
WDHD1; WD repeat and HMG-box DNA binding protein 1
Whamy
Windbeutel protein, N-terminal half
Wingless protein
wit
Wolf-Hirschhorn syndrome candidate 1
wound epithelium & transport / secretory cytoskeletal protein
wound epithelium & transport/secretory cell protein, 42 kDa
wrapper
Xenopus nuclear factor, xnf7
Xenotropic murine leukemia virus-related virus P12
X-prolyl aminopeptidase (aminopeptidase P) 1, soluble Peptide 1
X-prolyl aminopeptidase (aminopeptidase P) 1, soluble Peptide 2
Yan Drosophila protein
YAP1 (YAP65 / Yes-associated protein 1)
Y-box-binding protein 3
YBX1; Y box binding protein 1
YBX2; Y box binding protein 2
YEATS domain containing 4
YEATS domain-containing 4
YEATS2; YEATS domain containing 2
YY1 transcription repressor protein
YY1 transcriptional repressor protein; Yin-Yang-1
YY2 Transcription Factors
ZBTB16; Zinc finger and BTB domain containing 16
ZBTB2; Zinc finger and BTB domain containing 2
ZBTB25; Zinc finger and BTB domain containing 25
ZBTB5; Zinc finger and BTB domain containing 5
ZBTB5; Zinc finger and BTB domain containing 5
ZCCHC7; Zinc finger, CCHC domain containing 7
ZEB2; Zinc finger E-box binding homeobox 2
Zeta-chain (TCR) associated protein kinase 70kDa
zeugmatin
ZFP3 zinc finger protein
ZFP41 zinc finger protein
ZFP90; ZFP90 zinc finger protein
ZFP92 zinc finger protein
ZFYVE19; Zinc finger, FYVE domain containing 19
ZFYVE20; Zinc finger, FYVE domain containing 20
Zic family member 2
ZIC1; Zic family member 1
ZIM2; Zinc finger, imprinted 2
zinc alpha-2-glycoprotein (ZAG)
Zinc finger and BTB domain containing 18
Zinc finger and BTB domain containing 21
Zinc finger and BTB domain containing 37
Zinc finger and BTB domain containing 39
Zinc finger and BTB domain containing 46
Zinc finger and BTB domain containing 7B
Zinc finger and BTB domain containing 7C
Zinc finger and BTB domain containing protein 32
Zinc finger and SCAN domain containing 2
Zinc finger and SCAN domain containing 25
Zinc finger and SCAN domain containing 5A
Zinc finger and SCAN domain containing 9
Zinc finger and SCAN domain-containing protein 26
Zinc finger and SCAN domain-containing protein 29
Zinc finger CCCH domain-containing protein 15
Zinc finger CCCH-type containing 7A
Zinc finger CCHC domain-containing protein 7
Zinc finger E-box binding homeobox 2
Zinc finger family member 783
Zinc finger protein 134
Zinc finger protein 140
Zinc finger protein 155
Zinc finger protein 157
Zinc finger protein 165
Zinc finger protein 169
Zinc finger protein 18
Zinc finger protein 189
Zinc finger protein 200
Zinc finger protein 202
Zinc finger protein 207
Zinc finger protein 222
Zinc finger protein 230
Zinc finger protein 239
Zinc finger protein 239; ZNF239
Zinc finger protein 24
Zinc finger protein 263
Zinc finger protein 264
Zinc finger protein 280A
Zinc finger protein 280D
Zinc finger protein 333
Zinc finger protein 341
Zinc finger protein 354A
Zinc finger protein 354B
Zinc finger protein 358
Zinc finger protein 384
Zinc finger protein 385B
Zinc finger protein 397
Zinc finger protein 408
Zinc finger protein 410
Zinc finger protein 428
Zinc finger protein 438
Zinc finger protein 446
Zinc finger protein 467; ZNF467
Zinc finger protein 485
Zinc finger protein 496
Zinc finger protein 521
Zinc finger protein 526
Zinc finger protein 543
Zinc finger protein 548
Zinc finger protein 549
Zinc finger protein 550
Zinc finger protein 554
Zinc finger protein 574
Zinc finger protein 581
Zinc finger protein 583
Zinc finger protein 584
Zinc finger protein 597
Zinc finger protein 608
Zinc finger protein 623
Zinc finger protein 648
Zinc finger protein 654
Zinc finger protein 654; melanoma-associated antigen
Zinc finger protein 683
Zinc finger protein 696
Zinc finger protein 697
Zinc finger protein 701
Zinc finger protein 75a
Zinc finger protein 770
Zinc finger protein 784
Zinc finger protein 792
Zinc finger protein 8
Zinc finger protein 800
Zinc finger protein 81
Zinc finger protein Gfi-1
Zinc finger protein ZFAT
Zinc finger protein ZFPM2
Zinc finger with KRAB and SCAN domains 7
Zinc finger with KRAB and SCAN domains 8
Zinc Finger, AN1-type Domain 6
Zinc finger, BED-type containing 1
Zinc finger, BED-type containing 3
Zinc finger, FYVE domain containing 20 (Rabenosyn-5)
Zinc finger, imprinted 2
Zinc finger, matrin-type 2
Zinc finger, matrin-type 4
Zinc finger, MYM-type 3
Zinc finger, ZZ-type containing 3
Zinc fingers and homeoboxes 1
Zinc fingers and homeoboxes 2
Zinc fingers and homeoboxes 3
ZKSCAN1; Zinc finger with KRAB and SCAN domains 1
ZKSCAN2; Zinc finger with KRAB and SCAN domains 2
ZKSCAN3; Zinc finger with KRAB and SCAN domains 3
ZMYM3; Zinc finger, MYM-type 3
ZNF157; Zinc finger protein 157
ZNF165; Zinc finger protein 165
ZNF174; Zinc finger protein 174
ZNF175; Zinc finger protein 175
ZNF18; Zinc finger protein 18
ZNF192; Zinc finger with KRAB and SCAN domains 8
ZNF197; Zinc finger protein 197
ZNF202; Zinc finger protein 202
ZNF207; Zinc finger protein 207
ZNF212; Zinc finger protein 212
ZNF217; Zinc finger protein 217
ZNF23; Zinc finger protein 23
ZNF230; Zinc finger protein 230
ZNF232; Zinc finger protein 232
ZNF277; Zinc finger protein 277
ZNF296; Zinc finger protein 296
ZNF324; Zinc finger protein 324
ZNF324; Zinc finger protein 324
ZNF354A; Zinc finger protein 354A
ZNF384; Zinc finger protein 384
ZNF397; Zinc finger protein 397
ZNF410; Zinc finger protein 410
ZNF444; Zinc finger protein 444
ZNF446; Zinc finger protein 446
ZNF48; Zinc finger protein 48
ZNF483; Zinc finger protein 483
ZNF488; Zinc finger protein 488
ZNF503-AS2; Zinc finger protein 503-AS2
ZNF556; Zinc finger protein 556
ZNF585B; Zinc finger protein 585B
ZNF639; Zinc finger protein 639
ZNF689; Zinc finger protein 689
ZNF783; Zinc finger family member 783
ZNF784; Zinc finger protein 784
ZNF830; Zinc finger protein 830
ZNF846; Zinc finger protein 846
ZNFX1; Zinc finger, NFX1-type containing 1
ZO-1 tight junction protein
ZSCAN12; Zinc finger and SCAN domain containing 12
ZSCAN2; Zinc finger and SCAN domain containing 2
ZSCAN21; Zinc finger and SCAN domain containing 21
ZSCAN22; Zinc finger and SCAN domain containing 22
ZSCAN23; Zinc finger and SCAN domain containing 23
ZSCAN31; Zinc finger and SCAN domain containing 31
ZSCAN5A; Zinc finger and SCAN domain containing 5A
ZUFSP; Zinc finger with UFM1-specific peptidase domain
Zw5
ZXD family zinc finger C
ZXDC; ZXD family zinc finger C
ZZZ3; Zinc finger, ZZ-type containing 3

Major histocompatibility complex

The major histocompatibility complex (MHC) is a set of cell surface proteins essential for the acquired immune system to recognize foreign molecules in vertebrates, which in turn determines histocompatibility. The main function of MHC molecules is to bind to peptide fragments derived from pathogens and display them on the cell surface for recognition by the appropriate T-cells. MHC molecules mediate interactions of leukocytes, also called white blood cells (WBCs), which are immune cells, with other leukocytes or with body cells. The MHC determines compatibility of donors for organ transplant, as well as one’s susceptibility to an autoimmune disease via crossreacting immunization. The human MHC is also called the HLA (human leukocyte antigen) complex (often just the HLA). The mouse MHC is called the H-2 complex or H-2.

In a cell, protein molecules of the host’s own phenotype or of other biologic entities are continually synthesized and degraded. Each MHC molecule on the cell surface displays a molecular fraction of a protein, called an epitope. The presented antigen can be either self or non-self, thus preventing an organism’s immune system targeting its own cells. In its entirety, the MHC population is like a meter indicating the balance of proteins within the cell.

The MHC gene family is divided into three subgroups: class I, class II, and class III. Class I MHC molecules have β2 subunits so can only be recognised by CD8 co-receptors. Class II MHC molecules have no β2 subunits so can be recognised by CD4 co-receptors. In this way MHC molecules chaperone which type of lymphocytes may bind to the given antigen with high affinity, since different lymphocytes express different TCR co-receptors.

Diversity of antigen presentation, mediated by MHC classes I and II, is attained in at least three ways: (1) an organism’s MHC repertoire is polygenic (via multiple, interacting genes); MHC expression is codominant (from both sets of inherited alleles); MHC gene variants are highly polymorphic (diversely varying from organism to organism within a species). Major histocompatibility complex and sexual selection has been observed in male mice making mate choices of females with different MHCs and thus demonstrating sexual selection. Also, at least for MHC I presentation, there has been evidence of antigenic peptide splicing which can combine peptides from different proteins, vastly increasing antigen diversity.

In immunity

Of the three MHC classes identified, attention commonly focuses on classes I and II. By interacting with CD4 molecules on surfaces of helper T cells, MHC class II mediates establishment of specific immunity (also called acquired immunity or adaptive immunity). By interacting with CD8 molecules on surfaces of cytotoxic T cells, MHC class I mediates destruction of infected or malignant host cells, the aspect of specific immunity termed cellular immunity. (The other arm of specific immunity is humoral immunity, whose relation to MHC is more indirect)

Functions

MHC is the tissue-antigen that allows the immune system (more specifically T cells) to bind to, recognize, and tolerate itself (autorecognition). MHC is also the chaperone for intracellular peptides that are complexed with MHCs and presented to TCRs as potential foreign antigens. MHC interacts with TCR and its co-receptors to optimize binding conditions for the TCR-antigen interaction, in terms of antigen binding affinity and specificity, and signal transduction effectiveness.

Essentially, the MHC-peptide complex is a complex of autoantigen/alloantigen. Upon binding, T cells should in principle tolerate the auto-antigen, but activate when exposed to the allo-antigen. Disease states occur when this principle is disrupted.

Antigen presentation: MHC molecules bind to both T cell receptor and CD4/CD8 co-receptors on T lymphocytes, and the antigen epitope held in the peptide-binding groove of the MHC molecule interacts with the variable Ig-Like domain of the TCR to trigger T-cell activation.

Autoimmune reaction: Having some MHC molecules increases the risk of autoimmune diseases more than having others. HLA-B27 is an example. It is unclear how exactly having the HLA-B27 tissue type increases the risk of ankylosing spondylitis and other associated inflammatory diseases, but mechanisms involving aberrant antigen presentation or T cell activation have been hypothesized.

Tissue allorecognition: MHC molecules in complex with peptide epitopes are essentially ligands for TCR. T cells become activated by binding to the peptide-binding grooves of any MHC molecule that T cells were not entrained to recognize during thymus positive selection.

Lymphocytes

As a lineage of leukocytes, lymphocytes reside in peripheral lymphoid tissues, including lymphoid follicles and lymph nodes, and include B cells, T cells, and natural killer cells (NK cells). B cells, which act specifically, secrete antibody molecules, but do not bind MHC. T cells, which act specifically, as well as NK cells, which act innately, interact with MHC. NK cells express Killer Ig-like receptors (KIRs) that bind to MHC I molecules and signal through ITIM (immunoreceptor tyrosine inhibition motif) recruitment and activation of protein tyrosine phosphatases. This means in contrast to CD8/TCR interaction that activates Tc lymphocytes, NK cells becomes deactivated when bound to MHC I. When MHC class I expression is low, as is typically the case with abnormal cell function during viral infection or tumourigenesis, NK cells lose the inhibitory KIR signal and trigger programmed cell death of the abnormal cell. NK cells thus help prevent progress of cancerous cells by contributing to tumor surveillance.

MHC class II

MHC class II can be conditionally expressed by all cell types, but normally occurs only on professional antigen-presenting cells (APCs): macrophages, B cells, and especially dendritic cells (DCs). An APC takes up an antigen, performs antigen processing, and returns a molecular fraction of it—a fraction termed the epitope—to the APC’s surface, coupled within an MHC class II molecule mediating antigen presentation by displaying this epitope. On the cell’s surface, the epitope can contact its cognate region on immunologic structures recognizing that epitope. That molecular region which binds to—or, in jargon, ligates—the epitope is the paratope.

On surfaces of helper T cells are CD4 receptors, as well as T cell receptors (TCRs). When a naive helper T cell’s CD4 molecule docks to an APC’s MHC class II molecule, its TCR can meet and be imprinted by the epitope coupled within the MHC class II. This event primes the naive helper T cell. According to the local milieu, that is, the balance of cytokines secreted by APCs in the microenvironment, the naive helper T cell (Th0) polarizes into either a memory Th cell or an effector Th cell of phenotype either type 1 (Th1), type 2 (Th2), type 17 (Th17), or regulatory/suppressor (Treg), as so far identified, the Th cell’s terminal differentiation.

MHC class II thus mediates immunization to—or, if APCs polarize Th0 cells principally to Treg cells, immune tolerance of—an antigen. The polarization during primary exposure to an antigen is key in determining a number chronic diseases, such as inflammatory bowel diseases and asthma, by skewing the immune response that memory Th cells coordinate when their memory recall is triggered upon secondary exposure to similar antigens. (B cells express MHC class II to present antigen to Th0, but when their B cell receptors bind matching epitopes, interactions which are not mediated by MHC, these activated B cells secrete soluble immunoglobulins: antibody molecules mediating humoral immunity.)

MHC class I

MHC class I occurs on all nucleated cells and also in platelets—in essence all cells but red blood cells. It presents epitopes to killer T cells, also called cytotoxic T lymphocytes (CTLs). A CTL expresses CD8 receptors, in addition to TCRs. When a CTL’s CD8 receptor docks to a MHC class I molecule, if the CTL’s TCR fits the epitope within the MHC class I molecule, the CTL triggers the cell to undergo programmed cell death by apoptosis. Thus, MHC class I helps mediate cellular immunity, a primary means to address intracellular pathogens, such as viruses and some bacteria, including bacterial L forms, bacterial genus Mycoplasma, and bacterial genus Rickettsia. In humans, MHC class I comprises HLA-A, HLA-B, and HLA-C molecules.

Genes

MHC gene families are found in all vertebrates, though they vary widely. In humans, the MHC region occurs on chromosome 6, between the flanking genetic markers MOG and COL11A2 (from 6p22.1 to 6p21.3 about 29Mb to 33Mb on the hg19 assembly), and contains 240 genes spanning 3.6 megabase pairs (3 600 000 bases).[8] About half have known immune functions.

The same markers in the gray short-tailed opossum (Monodelphis domestica), a marsupial, span 3.95 Mb, yielding 114 genes, 87 shared with humans. Marsupial MHC genotypic variation lies between eutherian mammals and birds, taken as minimal MHC encoding, but is closer in organization to that of nonmammals, and MHC class I genes of marsupials have amplified within the class II region, yielding a unique class I/II region.

Class III functions very differently from class I and class II, but its locus occurs between the other two classes, on chromosome 6 in humans, and are frequently discussed together.

Class Encoding Expression
I (1) peptide-binding proteins, which select short sequences of amino acids for antigen presentation, as well as (2) molecules aiding antigen-processing (such as TAP and tapasin). One chain, called α, whose ligands are the CD8 receptor—borne notably by cytotoxic T cells—and inhibitory receptors borne by NK cells
II (1) peptide-binding proteins and (2) proteins assisting antigen loading onto MHC class II’s peptide-binding proteins (such as MHC II DM, MHC II DQ, MHC II DR, and MHC II DP). Two chains, called α & β, whose ligands are the CD4 receptors borne by helper T cells.
III Other immune proteins, outside antigen processing and presentation, such as components of the complement cascade (e.g., C2, C4, factor B), the cytokines of immune signaling (e.g., TNF-α), and heat shock proteinsbuffering cells from stresses Various
Proteins

MHC proteins have immunoglobulin-like structure.

MHC class I protein molecule

MHC Class I
MHC I occurs as an α chain composed of three domains—α1, α2, and α3. The α1 rests upon a unit of the non-MHC molecule β2 microglobulin(encoded on human chromosome 15). The α3 domain is transmembrane, anchoring the MHC class I molecule to the cell membrane. The peptide being presented is held by the floor of the peptide-binding groove, in the central region of the α1/α2 heterodimer (a molecule composed of two nonidentical subunits). The genetically encoded and expressed sequence of amino acids, the sequence of residues, of the peptide-binding groove’s floor determines which particular peptide residues it binds.

Classical MHC molecules present epitopes to the TCRs of CD8+ T lymphocytes. Nonclassical molecules (MHC class IB) exhibit limited polymorphism, expression patterns, and presented antigens; this group is subdivided into a group encoded within MHC loci (e.g., HLA-E, -F, -G), as well as those not (e.g., stress ligands such as ULBPs, Rae1, and H60); the antigen/ligand for many of these molecules remain unknown, but they can interact with each of CD8+ T cells, NKT cells, and NK cells.

MHC Class II

MHC class II is formed of two chains, α and β, each having two domains—α1 and α2 and β1 and β2—each chain having a transmembrane domain, α2 and β2, respectively, anchoring the MHC class II molecule to the cell membrane. The peptide-binding groove is formed of the heterodimer of α1 and β1.

MHC class II molecules in humans have five to six isotypes. Classic molecules present peptides to CD4+ lymphocytes. Nonclassic molecules, accessories, with intracellular functions, are not exposed on cell membranes, but in internal membranes in lysosomes, normally loading the antigenic peptides onto classic MHC class II molecules.

MHC Class III

Class III molecules have physiologic roles unlike classes I and II, but are encoded between them in the short arm of human chromosome 6. Class III molecules include several secreted proteins with immune functions: components of the complement system(such as C2, C4, and B factor), cytokines (such as TNF-α, LTA, and LTB), and heat shock proteins.

Antigen processing and presentation

MHC class I pathway: Proteins in the cytosol are degraded by the proteasome, liberating peptides internalized by TAPchannel in the endoplasmic reticulum, there associating with MHC-I molecules freshly synthesized. MHC-I/peptide complexes enter Golgi apparatus, are glycosylated, enter secretory vesicles, fuse with the cell membrane, and externalize on the cell membrane interacting with T lymphocytes.

Peptides are processed and presented by two classical pathways:

  • In MHC class II, phagocytessuch as macrophages and immature dendritic cells take up entities by phagocytosisinto phagosomes—though B cells exhibit the more general endocytosis into endosomes—which fuse with lysosomes whose acidic enzymes cleave the uptaken protein into many different peptides. Via physicochemical dynamics in molecular interaction with the particular MHC class II variants borne by the host, encoded in the host’s genome, a particular peptide exhibits immunodominanceand loads onto MHC class II molecules. These are trafficked to and externalized on the cell surface.
  • In MHC class I, any nucleated cell normally presents cytosolic peptides, mostly self peptides derived from protein turnover and defective ribosomal products. During viral infection, intracellular microorganism infection, or cancerous transformation, such proteins degraded in the proteosome are as well loaded onto MHC class I molecules and displayed on the cell surface. T lymphocytes can detect a peptide displayed at 0.1%-1% of the MHC molecules.

Peptide binding for Class I and Class II MHC molecules, showing the binding of peptides between the alpha-helix walls, upon a beta-sheet base. The difference in binding positions is shown. Class I primarily makes contact with backbone residues at the Carboxy and amino terminal regions, while Class II primarily makes contacts along the length of the residue backbone. The precise location of binding residues is determined by the MHC allele.
Table 2. Characteristics of the antigen processing pathways
Characteristic MHC-I pathway MHC-II pathway
Composition of the stable peptide-MHC complex Polymorphic chain α and β2 microglobulin, peptide bound to α chain Polymorphic chains α and β, peptide binds to both
Types of antigen presenting cells (APC) All nucleated cells Dendritic cells, mononuclear phagocytes, B lymphocytes, some endothelial cells, epithelium of thymus
T lymphocytes able to respond Cytotoxic T lymphocytes(CD8+) Helper T lymphocytes(CD4+)
Origin of antigenic proteins cytosolic proteins (mostly synthetized by the cell; may also enter from the extracellular medium via phagosomes) Proteins present in endosomes or lysosomes(mostly internalized from extracellular medium)
Enzymes responsible for peptide generation Cytosolic proteasome Proteases from endosomes and lysosomes (for instance, cathepsin)
Location of loading the peptide on the MHC molecule Endoplasmic reticulum Specialized vesicular compartment
Molecules implicated in transporting the peptides and loading them on the MHC molecules TAP (transporter associated with antigen processing) DM, invariant chain
T lymphocyte recognition restrictions

In their development in the thymus, T lymphocytes are selected to recognize MHC molecules of the host, but not recognize other self antigens. Following selection, each T lymphocyte shows dual specificity: The TCR recognizes self MHC, but only non-self antigens.

MHC restriction occurs during lymphocyte development in the thymus through a process known as positive selection. T cells that do not receive a positive survival signal — mediated mainly by thymic epithelial cells presenting self peptides bound to MHC molecules — to their TCR undergo apoptosis. Positive selection ensures that mature T cells can functionally recognize MHC molecules in the periphery (i.e. elsewhere in the body).

The TCRs of T lymphocytes recognise only sequential epitopes, also called linear epitopes, of only peptides and only if coupled within an MHC molecule. (Antibody molecules secreted by activated B cells, though, ligate diverse epitopes—peptide, lipid, carbohydrate, and nucleic acid—and recognize conformational epitopes, which have three-dimensional structure.)

In sexual mate selection
Main article: Major histocompatibility complex and sexual selection
See also: Interpersonal compatibility

MHC molecules enable immune system surveillance of the population of protein molecules in a host cell, and greater MHC diversity permits greater diversity of antigen presentation. In 1976, Yamazaki et al demonstrated a sexual selection mate choice by male mice for females of a different MHC. Similar results have been obtained with fish. Some data find lower rates of early pregnancy loss in human couples of dissimilar MHC genes.

MHC may be related to mate choice in some human populations, a theory that found support by studies by Ober and colleagues in 1997, as well as by Chaix and colleagues in 2008.[17] However, the latter findings have been controversial. If it exists, the phenomenon might be mediated by olfaction, as MHC phenotype appears strongly involved in the strength and pleasantness of perceived odour of compounds from sweat. Fatty acid esters—such as methyl undecanoate, methyl decanoate, methyl nonanoate, methyl octanoate, and methyl hexanoate—show strong connection to MHC.

In 1995, Claus Wedekind found that in a group of female college students who smelled T-shirts worn by male students for two nights (without deodorant, cologne, or scented soaps), by far most women chose shirts worn by men of dissimilar MHCs, a preference reversed if the women were on oral contraceptives. Results of a 2002 experiment likewise suggest HLA-associated odors influence odor preference and may mediate social cues. In 2005 in a group of 58 subjects, women were more indecisive when presented with MHCs like their own, although with oral contraceptives, the women showed no particular preference.[23] No studies show the extent to which odor preference determines mate selection (or vice versa).

Evolutionary diversity

Most mammals have MHC variants similar to those of humans, who bear great allelic diversity, especially among the nine classical genes—seemingly due largely to gene duplication—though human MHC regions have many pseudogenes. The most diverse loci, namely HLA-A, HLA-B, and HLA-DRB1, have roughly 1000, 1600, and 870 known alleles, respectively[citation needed]. Many HLA alleles are ancient, sometimes of greater homology to a chimpanzee MHC alleles than to some other human alleles of the same gene.

MHC allelic diversity has challenged evolutionary biologists for explanation. Most posit balancing selection (see polymorphism (biology)), which is any natural selection process whereby no single allele is absolutely most fit, such as frequency-dependent selectionand heterozygote advantage. Recent models suggest a high number of alleles is implausible via heterozygote advantage alone.[citation needed]

Pathogenic coevolution, a counterhypothesis, posits that common alleles are under greatest pathogenic pressure, driving positive selection of uncommon alleles—moving targets, so to say, for pathogens. As pathogenic pressure on the previously common alleles decreases, their frequency in the population stabilizes, and remain circulating in a large population. Despite great MHC polymorphism at the population level, an individual bears at most 18 MHC I or II alleles.

Relatively low MHC diversity has been observed in the cheetah (Acinonyx jubatus),[25]Eurasian beaver (Castor fiber),[26] and giant panda (Ailuropoda melanoleuca).[27] In 2007 low MHC diversity was attributed a role in disease susceptibility in the Tasmanian devil(Sarcophilus harrisii), native to the isolated island of Tasmania, such that an antigen of a transmissible tumor, involved in devil facial tumour disease, appears to be recognized as a self antigen.[28] To offset inbreeding, efforts to sustain genetic diversity in populations of endangered species and of captive animals have been suggested.

In transplant rejection

In a transplant procedure, as of an organ or stem cells, MHC molecules act themselves as antigens and can provoke immune response in the recipient, thus causing transplant rejection. MHC molecules were identified and named after their role in transplantrejection between mice of different strains, though it took over 20 years to clarify MHC’s role in presenting peptide antigens to cytotoxic T lymphocytes (CTLs).

Each human cell expresses six MHC class I alleles (one HLA-A, -B, and -C allele from each parent) and six to eight MHC class II alleles (one HLA-DP and -DQ, and one or two HLA-DR from each parent, and combinations of these). The MHC variation in the human population is high, at least 350 alleles for HLA-A genes, 620 alleles for HLA-B, 400 alleles for DR, and 90 alleles for DQ. Any two individuals who are not identical twins will express differing MHC molecules. All MHC molecules can mediate transplant rejection, but HLA-C and HLA-DP, showing low polymorphism, seem least important.[clarification needed]

When maturing in the thymus, T lymphocytes are selected for their TCR incapacity to recognize self antigens, yet T lymphocytes can react against the donor MHC’s peptide-binding groove, the variable region of MHC holding the presented antigen’s epitope for recognition by TCR, the matching paratope. T lymphocytes of the recipient take the incompatible peptide-binding groove as nonself antigen. The T lymphocytes’ recognition of the foreign MHC as self is allorecognition.

Transplant rejection has various types known to be mediated by MHC (HLA):

  • Hyperacute rejection occurs when, before the transplantation, the recipient has preformed anti-HLA antibodies, perhaps by previous blood transfusions (donor tissue that includes lymphocytes expressing HLA molecules), by anti-HLA generated during pregnancy (directed at the father’s HLA displayed by the fetus), or by previous transplantation;
  • Acute cellular rejection occurs when the recipient’s T lymphocytes are activated by the donor tissue, causing damage via mechanisms such as direct cytotoxicity from CD8 cells.
  • Acute humoral rejection and chronic disfunction occurs when the recipient’s anti-HLA antibodies form directed at HLA molecules present on endothelial cells of the transplanted tissue.

In all of the above situations, immunity is directed at the transplanted organ, sustaining lesions. A cross-reaction test between potential donor cells and recipient serum seeks to detect presence of preformed anti-HLA antibodies in the potential recipient that recognize donor HLA molecules, so as to prevent hyperacute rejection. In normal circumstances, compatibility between HLA-A, -B, and -DR molecules is assessed. The higher the number of incompatibilities, the lower the five-year survival rate. Global databases of donor information enhance the search for compatible donors.

HLA biology

Human MHC class I and II are also called human leukocyte antigen(HLA). To clarify the usage, some of the biomedical literature uses HLA to refer specifically to the HLA protein molecules and reserves MHC for the region of the genome that encodes for this molecule, but this is not a consistent convention.

The most studied HLA genes are the nine classical MHC genes: HLA-A, HLA-B, HLA-C, HLA-DPA1, HLA-DPB1, HLA-DQA1, HLA-DQB1, HLA-DRA, and HLA-DRB1. In humans, the MHC gene cluster is divided into three regions: classes I, II, and III. The A, B and C genes belong to MHC class I, whereas the six D genes belong to class II.

MHC alleles are expressed in codominant fashion.[11] This means the alleles (variants) inherited from both parents are expressed equally:

  • Each person carries 2 alleles of each of the 3 class-I genes, (HLA-A, HLA-B and HLA-C), and so can express six different types of MHC-I (see figure).
  • In the class-II locus, each person inherits a pair of HLA-DP genes (DPA1 and DPB1, which encode α and β chains), a couple of genes HLA-DQ (DQA1 and DQB1, for α and β chains), one gene HLA-DRα (DRA1), and one or more genes HLA-DRβ (DRB1and DRB3, -4 or -5). That means that one heterozygous individual can inherit six or eight functioning class-II alleles, three or more from each parent. The role of DQA2or DQB2 is not verified. The DRB2, DRB6, DRB7, DRB8 and DRB9 are pseudogenes.

The set of alleles that is present in each chromosome is called the MHC haplotype. In humans, each HLA allele is named with a number. For instance, for a given individual, his haplotype might be HLA-A2, HLA-B5, HLA-DR3, etc… Each heterozygous individual will have two MHC haplotypes, one each from the paternal and maternal chromosomes.

The MHC genes are highly polymorphic; many different alleles exist in the different individuals inside a population. The polymorphism is so high, in a mixed population (nonendogamic), no two individuals have exactly the same set of MHC molecules, with the exception of identical twins.

The polymorphic regions in each allele are located in the region for peptide contact. Of all the peptides that could be displayed by MHC, only a subset will bind strongly enough to any given HLA allele, so by carrying two alleles for each gene, a much larger set of peptides can be presented.[why?]

On the other hand, inside a population, the presence of many different alleles ensures there will always be an individual with a specific MHC molecule able to load the correct peptide to recognize a specific microbe. The evolution of the MHC polymorphism ensures that a population will not succumb to a new pathogen or a mutated one, because at least some individuals will be able to develop an adequate immune response to win over the pathogen. The variations in the MHC molecules (responsible for the polymorphism) are the result of the inheritance of different MHC molecules, and they are not induced by recombination, as it is the case for the antigen receptors.

Because of the high levels of allelic diversity found within its genes, MHC has also attracted the attention of many evolutionary biologists.

Immunoglobulin superfamily

The immunoglobulin superfamily (IgSF) is a large group of cell surface and soluble proteins that are involved in the recognition, binding, or adhesion processes of cells. Molecules are categorized as members of this superfamily based on shared structural features with immunoglobulins (also known as antibodies); they all possess a domain known as an immunoglobulin domain or fold. Members of the IgSF include cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins. They are commonly associated with roles in the immune system. The sperm-specific protein Izumo, a member of the immunoglobulin superfamily, has also been identified as the only sperm membrane protein essential for sperm-egg fusion.

Immunoglobulin domains

Proteins of the IgSF possess a structural domain known as an immunoglobulin (Ig) domain. Ig domains are named after the immunoglobulin molecules. They contain about 70-110 amino acids and are categorized according to their size and function. Ig-domains possess a characteristic Ig-fold, which has a sandwich-like structure formed by two sheets of antiparallel beta strands. Interactions between hydrophobic amino acids on the inner side of the sandwich and highly conserved disulfide bonds formed between cysteine residues in the B and F strands, stabilize the Ig-fold. One end of the Ig domain has a section called the complementarity determining region that is important for the specificity of antibodies for their ligands.

Classification

The Ig like domains can be classified as IgV, IgC1, IgC2, or IgI.

Most Ig domains are either variable (IgV) or constant (IgC).

IgV: IgV domains with 9 beta strands are generally longer than IgC domains with 7 beta strands.
IgC1 and IgC2: Ig domains of some members of the IgSF resemble IgV domains in the amino acid sequence, yet are similar in size to IgC domains. These are called IgC2 domains, while standard IgC domains are called IgC1 domains.
IgI: Other Ig domains exist that are called intermediate (I) domains.

Members of the immunoglobulin superfamily

The Ig domain was reported to be the most populous family of proteins in the human genome with 765 members identified. Members of the family can be found even in the bodies of animals with a simple physiological structure such as poriferan sponges. They have also been found in bacteria, where their presence is thought to be due to horizontal gene transfer.

Members of the immunoglobulin superfamily
Molecule function/category Examples Description
Antigen receptors
  • Antibodies or immunoglobulins
  • T cell receptor chains
Antigen receptors found on the surface of T and B lymphocytes in all jawed vertebrates belong to the IgSF. Immunoglobulin molecules (the antigen receptors of B cells) are the founding members of the IgSF. In humans, there are five distinct types of immunoglobulinmolecule all containing a heavy chain with four Ig domains and a light chain with two Ig domains. The antigen receptor of T cells is the T cell receptor (TCR), which is composed of two chains, either the TCR-alpha and -beta chains, or the TCR-delta and gamma chains. All TCR chains contain two Ig domains in the extracellular portion; one IgV domain at the N-terminus and one IgC1 domain adjacent to the cell membrane.
Antigen presentingmolecules
  • Class I MHC
  • Class II MHC
  • beta-2 microglobulin
The ligands for TCRs are major histocompatibility complex (MHC) proteins. These come in two forms; MHC class I forms a dimer with a molecule called beta-2 microglobulin (β2M) and interacts with the TCR on cytotoxic T cells and MHC class II has two chains (alpha and beta) that interact with the TCR on helper T cells. MHC class I, MHC class II and β2M molecules all possess Ig domains and are therefore also members of the IgSF.
Co-receptors
  • CD4
  • CD8
  • CD19
Co-receptors and accessory molecules: Other molecules on the surfaces of T cells also interact with MHC molecules during TCR engagement. These are known as co-receptors. In lymphocyte populations, the co-receptor CD4is found on helper T cells and the co-receptor CD8 is found on cytotoxic T cells. CD4 has four Ig domains in its extracellular portion and functions as a monomer. CD8, in contrast, functions as a dimer with either two identical alpha chains or, more typically, with an alpha and beta chain. CD8-alpha and CD8-beta each has one extracellular IgV domain in its extracellular portion. A co-receptor complex is also used by the BCR, including CD19, an IgSF molecule with two IgC2-domains.
Antigen receptor accessory molecules
  • CD3-γ, -δ and -ε chains
  • CD79a and CD79b
A further molecule is found on the surface of T cells that is also involved in signaling from the TCR. CD3 is a molecule that helps to transmit a signal from the TCR following its interaction with MHC molecules. Three different chains make up CD3 in humans, the gamma chain, delta chain and epsilon chain, all of which are IgSF molecules with a single Ig domain.Similar to the situation with T cells, B cells also have cell surface co-receptors and accessory molecules that assist with cell activation by the B Cell Receptor (BCR)/immunoglobulin. Two chains are used or signaling, CD79a and CD79b that both possess a single Ig domain.
Co-stimulatory or inhibitory molecules
  • CD28
  • CD80 and CD86 (also known as B7.1 and B7.2 molecules)
Co-stimulatory or inhibitory molecules: Co-stimulatory and inhibitory signaling receptors and ligands control the activation, expansion and effector functions of cells. One major group of IgSF co-stimulatory receptors are molecules of the CD28 family; CD28, CTLA-4, program death-1 (PD-1), the B- and T-lymphocyte attenuator (BTLA, CD272), and the inducible T-cell co-stimulator (ICOS, CD278);[7] and their IgSF ligands belong to the B7 family; CD80 (B7-1), CD86 (B7-2), ICOS ligand, PD-L1 (B7-H1), PD-L2 (B7-DC), B7-H3, and B7-H4 (B7x/B7-S1).[8]
Receptors on Natural killer cells
  • Killer-cell immunoglobulin-like receptors (KIR)
Receptors on Leukocytes
  • Leukocyte immunoglobulin-like receptors (LILR)
IgSF CAMs
  • NCAMs
  • ICAM-1
  • CD2 subset
  • Type IIa and Type IIb RPTPs, described in Receptor tyrosine kinases/phosphatases subsection below
  • CD2 subset of IgSF represented large group of homologous cell adhesion molecules (CAMs), includes CD2, CD58, CD48, CD150, CD229 and CD244.[9][10][11]
Cytokine receptors
  • Interleukin-6 receptor
  • Colony stimulating factor 1 receptor
Growth factor receptors
  • Platelet-derived growth factor receptor(PDGFR)
  • Mast/stem cell growth factor receptor precursor (SCFR, c-kit, CD117 antigen)
Receptor tyrosine kinases/phosphatases
  • Tyrosine-protein kinase receptor Tie-1 precursor
  • Type IIa and Type IIb Receptor protein tyrosine phosphatases(RPTPs), including, but not limited to, PTPRM, PTPRK, PTPRU, PTPRD, PTPRF
Ig binding receptors
  • polymeric immunoglobulin receptor (PIGR)
  • Some Fc receptors
Others
  • CD147
  • CD90
  • CD7
  • Butyrophilins (Btn)
  • Titin

 

MHC class I

MHC class I molecules are one of two primary classes of major histocompatibility complex (MHC) molecules (the other being MHC class II) and are found on the cell surface of all nucleated cells in the bodies of jawed vertebrates. They also occur on platelets, but not on red blood cells. Their function is to display peptide fragments of non-self proteins from within the cell to cytotoxic T cells; this will trigger an immediate response from the immune system against a particular non-self antigen displayed with the help of an MHC class I protein. Because MHC class I molecules present peptides derived from cytosolic proteins, the pathway of MHC class I presentation is often called cytosolic or endogenous pathway.

Function

Class I MHC molecules bind peptides generated mainly from degradation of cytosolic proteins by the proteasome. The MHC I:peptide complex is then inserted via endoplasmic reticulum into the external plasma membrane of the cell. The epitope peptide is bound on extracellular parts of the class I MHC molecule. Thus, the function of the class I MHC is to display intracellular proteins to cytotoxic T cells (CTLs). However, class I MHC can also present peptides generated from exogenous proteins, in a process known as cross-presentation.

A normal cell will display peptides from normal cellular protein turnover on its class I MHC, and CTLs will not be activated in response to them due to central and peripheral tolerance mechanisms. When a cell expresses foreign proteins, such as after viral infection, a fraction of the class I MHC will display these peptides on the cell surface. Consequently, CTLs specific for the MHC:peptide complex will recognize and kill presenting cells.

Alternatively, class I MHC itself can serve as an inhibitory ligand for natural killer cells (NKs). Reduction in the normal levels of surface class I MHC, a mechanism employed by some viruses during immune evasion or in certain tumors, will activate NK cell killing.

 

Locus

A locus (plural loci) in genetics is the position of a gene on a chromosome. Each chromosome carries many genes; humans’ estimated ‘haploid’ protein coding genes are 19,000-20,000,[2] on the 23 different chromosomes. A variant of the similar DNA sequence located at a given locus is called an allele. The ordered list of loci known for a particular genome is called a gene map. Gene mapping is the process of determining the locus for a particular biological trait.

Diploid and polyploid cells whose chromosomes have the same allele of a given gene at some locus are called homozygous with respect to that gene, while those that have different alleles of a given gene at a locus, are called heterozygous with respect to that gene.

Nomenclature

The chromosomal locus of a gene might be written “6p21.3”. Because “21” refers to “region 2, band 1” this is read as “two one”, not as “twenty-one”. So the entire locus is “six P two one point three.”

Component Explanation
6 The chromosome number.
p The position is on the chromosome’s short arm (a common apocryphal explanation is that the p stands for petit in French); qindicates the long arm (chosen as next letter in alphabet after p; alternatively it is sometimes said that q stands for queuemeaning tail in French).
21.3 The numbers that follow the letter represent the position on the arm: region 2, band 1, sub-band 3. The bands are visible under a microscope when chromosome is suitably stained. Each of the bands is numbered, beginning with 1 for the band nearest the centromere. Sub-bands and sub-sub-bands are visible at higher resolution.

A range of loci is specified in a similar way. For example, the locus of gene OCA1 may be written “11q1.4-q2.1”, meaning it is on the long arm of chromosome 11, somewhere in the range from sub-band 4 of region 1 to sub-band 1 of region 2.

The ends of a chromosome are labeled “pter” and “qter”, and so “2qter” refers to the terminus of the long arm of chromosome 2.

Centisome

A centisome (not to be confused with a centrosome) is defined as 1% of a chromosome length.

Liste des allèles humains d’antigène leucocytaire associés aux affections cutanées

Il existe de nombreux allèles de l’antigène leucocytaire humain (HLA) associés à des affections ou affectant le système tégumentaire humain

Condition Associated HLA allele(s)
Fixed drug eruption B22
Lichen planus DR1
DR2
DRw9
DR10
Bw15
B8
Psoriasis Cw6
DR406
Psoriatic arthritis B27
Ankylosing spondylitis B27
Reactive arthritis B27
Acute anterior uveitis B27
Behçet’s disease B51
Dermatitis herpetiformis DQw2
DR3
B8
Pemphigus vulgaris DR4
DRw6
Dw10
Herpes gestationis DR3
DR4
Epidermolysis bullosa acquisita DR2
Subacute cutaneous lupus erythematosus DR3
Dermatomyositis DQA1
DR3
B8
DRw52
Alopecia areata DR5
Sjögren’s syndrome DR3
DQ2
Herpes simplex virus-related erythema multiforme B12
Chronic idiopathic urticaria DR4
DQ8
Actinic prurigo DR4 subtype DRB1*0407
Systemic lupus erythematosus DR3
DR2
Generalized granuloma annulare Bw35
Lichen sclerosus DQ7
Early onset and severe psoriasis B17
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