MAG / Siglec-4a

MAG / Siglec-4a Molekülinformation

Englischer Name	Myelin-associated glycoprotein	Anzahl der inverkehr gebrachten Arzneimittel	0
Anzahl der klinischen Arzneimittel	1	Target-Alias	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
Höchste Forschungs- und Entwicklungsphase	Phase 2 Clinical

Englischer Name	Myelin-associated glycoprotein
Target-Alias	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
Anzahl der inverkehr gebrachten Arzneimittel	0
Anzahl der klinischen Arzneimittel	1
Höchste Forschungs- und Entwicklungsphase	Phase 2 Clinical

MAG / Siglec-4a Produktliste

Attribut
Protein (4)
Produktbibliothek
Online (4)
Spezies
Human (3)Mouse (1)
Etikett
His Tag (1)Fc Tag (1)His Tag & Avi Tag (2)
Marker
Unconjugated (2)Biotin-labeled (2)

Produktnummer	Spezies	Expressionssystem	Produktbeschreibung	Vorbestellen/Bestellen
HOT MAG-H5254	Human	HEK293	Human MAG / Siglec-4a Protein, Fc Tag	In den Warenkorb legen
HOT MAG-H52H8	Human	HEK293	Human MAG / Siglec-4a Protein, His Tag	In den Warenkorb legen
HOT MAG-H82E9	Human	HEK293	Biotinylated Human MAG / Siglec-4a Protein, His,Avitag™	In den Warenkorb legen
MAG-M82E9	Mouse	HEK293	Biotinylated Mouse MAG / Siglec-4a Protein, His,Avitag™ (MALS verified)	In den Warenkorb legen

Gesamtmenge4

MAG / Siglec-4a Molekülhintergrund

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.