MAG / Siglec-4a

MAG / Siglec-4a Informations sur la molécule

Nom anglais	Myelin-associated glycoprotein	Nombre de médicaments commercialisés	0
Nombre de médicaments cliniques	1	Alias de la cible	MAG，Siglec-4a，GMA，Sialic Acid Binding Ig-Like Lectin 4A，Myelin-Associated Glycoprotein，SIGLEC4A，S-MAG，SPG75，Myelin Associated Glycoprotein，Sialic Acid-Binding Immunoglobulin-Like Lectin 4A
Phase de R&D la plus avancée	Phase 2 Clinical

Nom anglais	Myelin-associated glycoprotein
Alias de la cible	MAG，Siglec-4a，GMA，Sialic Acid Binding Ig-Like Lectin 4A，Myelin-Associated Glycoprotein，SIGLEC4A，S-MAG，SPG75，Myelin Associated Glycoprotein，Sialic Acid-Binding Immunoglobulin-Like Lectin 4A
Nombre de médicaments commercialisés	0
Nombre de médicaments cliniques	1
Phase de R&D la plus avancée	Phase 2 Clinical

MAG / Siglec-4a Liste de produits

Attribut
Protein (4)
Bibliothèque de produits
En ligne (4)
Espèces
Human (3)Mouse (1)
Étiquette
His Tag (1)Fc Tag (1)His Tag & Avi Tag (2)
Marqueur
Unconjugated (2)Biotin-labeled (2)

Numéro de produit	Espèces	Système d'expression	Description du produit	Pré-commande/Commande
HOT MAG-H5254	Human	HEK293	Human MAG / Siglec-4a Protein, Fc Tag	Ajouter au panier
HOT MAG-H52H8	Human	HEK293	Human MAG / Siglec-4a Protein, His Tag	Ajouter au panier
HOT MAG-H82E9	Human	HEK293	Biotinylated Human MAG / Siglec-4a Protein, His,Avitag™	Ajouter au panier
MAG-M82E9	Mouse	HEK293	Biotinylated Mouse MAG / Siglec-4a Protein, His,Avitag™ (MALS verified)	Ajouter au panier

Quantité totale4

MAG / Siglec-4aContexte de la molécule

Myelin-associated glycoprotein (MAG), a nervous system cell adhesion molecule, is an I-type lectin that binds to sialylated glycoconjugates, including gangliosides bearing characteristic structural determinants. Preferentially binds to alpha-2,3-linked sialic acid. Binds ganglioside Gt1b. Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2. Protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. In dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides. In cerebellar granule cells the inhibition is mediated primarily via binding to neuronal gangliosides. In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides.