Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Recombinant Human MOG, immobilized at 1 μg/mL on a 96-well plate, is able to significantly enhance neurite outgrowth.
Source
Mouse myeloma cell line, NS0-derived human MOG protein Gly30-Gly154, with a substitution at Asp131Ala and a C-terminal 10-His tag
>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
Bioactivity
Theoretical MW
16 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.
SDS-PAGE
20-30 kDa, reducing conditions
Publications
Read Publication using 8535-MO 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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 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 MOG Protein, CF
MGC26137
MOG Ig-AluB
MOG
MOGIG2
myelin oligodendrocyte glycoprotein
myelin-oligodendrocyte glycoprotein
Background
Myelin oligodendrocyte glycoprotein (MOG) is 28 kDa single-pass transmembrane glycoprotein that is a member of the Ig superfamily (1, 2). Human MOG is synthesized with a 29 amino acid (aa) signal sequence, a 125 aa extracellular domain (ECD) containing an Ig-like domain, a 21 aa transmembrane domain, and a 72 aa cytosolic fragment featuring a hydrophobic domain that associates with the cytoplasmic face of the plasma membrane. The ECD of mature human MOG shares 90% aa sequence identity with the ECD of both mouse and rat MOG. Unlike mouse and rat, human MOG has seven splice variants, including a soluble ECD isoform and multiple isoforms that have a truncated cytoplasmic domain (3, 4). Dimerization of MOG occurs via the extracellular Ig-like domain (5-8). MOG is expressed exclusively by oligodendrocytes in the central nervous system (CNS) and is localized to the outer layer of the myelin sheath as well as in the oligodendrocyte plasma membrane (9). MOG expression in the brain can be used as a temporal biomarker for myelin development. MOG is an important antigenic target for autoimmune diseases that mediate demyelination in the CNS (10). In vivo administration of exogenous MOG protein or peptide induces experimental autoimmune encephalomyelitis (EAE) in multiple animal species (11, 12). EAE is used as an animal model for multiple sclerosis and related CNS demyelinating diseases. MOG is thought to function as an adhesion molecule as well as a mediator of immune activation in the CNS (9, 13).
Johns, T.G. and C.C. Bernard (1999) J. Neurochem. 72:1.
Pham-Dinh, D. et al. (1993) Proc. Natl. Acad. Sci. U S A 90:7990.
Hilton, A.A. et al. (1995) J. Neurochem. 65:309.
Slavin, A.J. et al. (1997) Dev. Neurosci. 19:69.
Abo, S. et al. (1993) Biochem. Mol. Biol. Int. 30:945.
Amiguet, P. et al. (1992) J. Neurochem. 58:1676.
Bettadapura, J. et al. (1998) J. Neurochem. 70:1593.
Clements, C.S. et al. (2003) Proc. Natl. Acad. Sci. U S A 100:11059.
Reindl, M. et al. (2013) Nat. Rev. Neurol. 9:455.
von Budingen, H.C. et al. (2004) Eur. J. Immunol. 34:2072.
Rangachari, M. and V.K. Kuchroo (2013) J. Autoimmun. 45:31.
Tompkins, S.M. et al. (2002) J. Immunol. 168:4173.
Garcia-Vallejo, J.J. et al. (2014) J. Exp. Med. 211:1465.
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