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Your Position: Home > All Other Proteins > MAG / Siglec-4a > MAG-H5254

Human MAG / Siglec-4a Protein, Fc Tag

  • Synonym
    MAG,Siglec-4a,GMA,S-MAG
  • Source
    Human MAG, Fc Tag (MAG-H5254) is expressed from human 293 cells (HEK293). It contains AA Gly 20 - Pro 516 (Accession # P20916-1).
    Predicted N-terminus: Gly 20
  • Molecular Characterization
    Online(Gly 20 - Pro 516) P20916-1

    This protein carries a human IgG1 Fc tag at the C-terminus.

    The protein has a calculated MW of 81.1 kDa. The protein migrates as 100-115 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

    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.

  • Storage

    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:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Human MAG, Fc Tag (Cat. No. MAG-H5254) SDS-PAGE gel

Human MAG, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.

  • 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.
  • References
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

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Price(USD) : $300.00

Price(USD) : $1980.00

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