Recombinant Human 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. When immobilized as a 3 µL droplet containing 200 ng on a nitrocellulose coated microplate, Recombinant Human MAG/Siglec‑4a Fc Chimera is able to significantly inhibit neurite outgrowth. |
Source |
Human embryonic kidney cell, HEK293-derived human MAG/Siglec-4a protein Human MAG (Gly20-Pro516) Accession # P20916 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gly20 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
MAG |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
81 kDa. 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. |
Packaging, Storage & Formulations
Storage |
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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
500 µg/mL in PBS |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human MAG/Siglec-4a Fc Chimera Protein, CF
Background
Myelin-Associated Glycoprotein (MAG), also known as Siglec-4a, is a type I transmembrane glycoprotein belonging to the Siglec family, a subgroup of the Ig superfamily (1). It is composed of an extracellular segment containing five Ig-like domains, a single transmembrane segment, and a cytoplasmic domain. Mature MAG exists as two isoforms, termed S-MAG (short) and L-MAG (long), due to alternative splicing of the cytoplasmic domain (1, 2). S-MAG has a predicted molecular weight of 67 kDa while L-MAG has a predicted molecular weight of 71 kDa (1, 2). Additionally, proteolytic cleavage of the extracellular domain produces a soluble MAG (3). Within shared regions in the extracellular domain, human MAG shares 95% aa sequence identity with mouse and rat MAG. MAG functions as an adhesion molecule during neural development. It preferentially binds to alpha -2,3-linked sialic acid terminal structures found on cell surface molecules (1, 4, 5). MAG is selectively expressed by myelinating oligodendrocytes and Schwann cells and plays an important role in axon-myelin stability (1, 4). Specifically, L-MAG is involved in myelination in the central nervous system (CNS) while S-MAG is the predominate isoform expressed during myelination in the peripheral nervous system (1). MAG is also reported to regulate the axon cytoskeleton and support the distribution of axon molecules at the nodes of Ranvier (1, 4). In addition, it has been identified as a major inhibitor of neurite outgrowth (1, 4, 6). However, MAG has also been reported to protect neurons from excitotoxicity (1, 7). MAG is believed to utilize the gangliosides GD1a and GT1b, the Nogo receptors NgR1 and NgR2/NgRH1, Integrin beta 1/CD29, and PIR-B to mediate its effects (1, 4, 5, 8, 9). Soluble MAG, which is released from myelin in large quantities, has been identified in normal human tissues and in tissues from patients with neurological disorders (3). It is believed that this soluble MAG might contribute to the lack of CNS neuron regeneration after injury (3).
- Lopez, P.H. (2014) Adv. Neurobiol. 9:245.
- Salzer, J.L. et al. (1987) J. Cell Biol. 104:957.
- Tang, S. et al. (1997) Mol. Cell. Neurosci. 9:333.
- Schnaar, R.L. and P.H. Lopez (2009) J. Neurosci. Res. 87:3267.
- Schnaar, R.L. (2010) FEBS Lett. 584:1741.
- Akbik, F. et al. (2012) Exp. Neurol. 235:43.
- Lopez, P.H. et al. (2011) J. Neurochem. 116:900.
- Atwal, J.K. et al. (2008) Science 322:967.
- Goh, E.L. et al. (2008) Mol. Brain 1:10.
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