Biotinylated Human MAG / Siglec-4a Protein, His,Avitag™

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MAG-H82E9-25ug
$360.00
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MAG-H82E9-200ug
$1,565.00
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MAG-H82E9
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Synonyms

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

Source

Biotinylated Human MAG, His,Avitag (MAG-H82E9) is expressed from human 293 cells (HEK293). It contains AA Gly 20 - Pro 516 (Accession # P20916-1).

Predicted N-terminus: Gly 20

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™).

The protein has a calculated MW of 58.3 kDa. The protein migrates as 80-90 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Labeling

Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.

Protein Ratio

Passed as determined by the SABA assay / HABA assay / binding ELISA.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, 0.5 M Arginine, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

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.