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Your Position: Home > MAG / Siglec-4a

MAG / Siglec-4a

Brief Information

Name:Myelin-associated glycoprotein
Target Synonym: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
Number of Launched Drugs:0
Number of Drugs in Clinical Trials:1
Lastest Research Phase:Phase 2 Clinical

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Cat. No. Species Product Description Structure Purity Feature
MAG-M82E9 Mouse Biotinylated Mouse MAG / Siglec-4a Protein, His,Avitag™ (MALS verified)
MAG-M82E9-structure
MAG-M82E9-sds
MAG-H82E9 Human Biotinylated Human MAG / Siglec-4a Protein, His,Avitag™
MAG-H82E9-structure
MAG-H82E9-sds
MAG-H5254 Human Human MAG / Siglec-4a Protein, Fc Tag
MAG-H5254-structure
MAG-H5254-sds
MAG-H52H8 Human Human MAG / Siglec-4a Protein, His Tag
MAG-H52H8-structure
MAG-H52H8-sds
ACRO Quality

Part of Bioactivity data

MAG-H5254-SPR
MAG / Siglec-4a SPR

Human Nogo Receptor, His Tag (Cat. No. NOR-H52H3) capture on NTA-Series S sensor chip can bind Human MAG, Fc Tag (Cat. No. MAG-H5254) with an affinity constant of 2.21 μM as determined in a SPR assay (Biacore 8K) (Routinely tested).

Protocol
MAG-M82E9-MALS-HPLC
MAG / Siglec-4a MALS images

The purity of Biotinylated Mouse MAG, His,Avitag (Cat. No. MAG-M82E9) is more than 90% and the molecular weight of this protein is around 120-150 kDa verified by SEC-MALS.

Synonym Name

MAG,Siglec-4a,GMA,S-MAG

Background

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.

Clinical and Translational Updates

Clinical Drug Information

Name Research Code Research Phase Company Indications Clinical Trials
AXER-204 AXER-204 Phase 2 Clinical Renetx Bio Inc Cardiovascular Diseases Details

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