Recombinant Rat MAG/Siglec-4a Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit neurite outgrowth of dissociated E13 chick embryonic dorsal root ganglia (DRG) neurons. Able to significantly inhibit neurite outgrowth when immobilized as a 3 µL droplet containing 400 ng on a nitrocellulose-coated microplate.
Source
Mouse myeloma cell line, NS0-derived rat MAG/Siglec-4a protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.1 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Theoretical MW
81 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
120 kDa, reducing conditions
Publications
Read Publications using 538-MG in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat MAG/Siglec-4a Fc Chimera Protein, CF
GMAsialic acid binding Ig-like lectin 4A
MAG
myelin associated glycoprotein
myelin-associated glycoprotein
sialic acid-binding immunoglobulin-like lectin 4A
Siglec4a
Siglec-4a
S-MAG
Background
MAG (Myelin-Associated Glycoprotein), a type I transmembrane glycoprotein containing five Ig-like domains in its extracellular domain is an adhesion molecule belonging to the immunoglobin superfamily. Within this superfamily, MAG, CD22, CD33, Schwann cell myelin protein, and sialoadhesin which bind specifically to cell-surface glycan containing sialic acid residues define the I-type sialyl lectin subgroup, also called the sialoadhesin family. Sialoadhesins mediate diverse biological processes through recognition of specific sialyted glycans on cell surface. MAG is expressed on myelinating oligodenrocytes and Schwann cells, and preferentially recognizes alpha 2, 3-linked sialic acid on O-linked glycans and gangliosides. MAG exists as two isoforms which differ in the sequence and length of the cytoplasmic tail. The large form (71 kDa) and small form (67 kDa) arise from alternative spliced mRNAs. Although MAG might encounter haematopoietic cells and lymphocytes under pathologic conditions, it would normally be expected to interact with neuronal cells. It has been shown that MAG promotes axonal growth from neonatal DRG neurons and embryonic spinal neurons, but is a potent inhibitor of axonal re-growth from adult DRG and postnatal cerebellar neurons. MAG plays an important role in the interaction between axons and myelin. A soluble form of MAG containing the extracellular domain is released from myelin in large quantities and identified in normal human tissues and in tissues from patients with neurological disorders. This soluble MAG might contribute to the lack of CNS neuron regeneration after injury.
Kelm, S. et al. (1994) Current Biology 4:965.
McKerracher, L. et al. (1994) Neuron 13:805.
Tang, S. et al. (1997) Molecular and Cellular Neuroscience 9:333.
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