MOG (35-51) cit46 human MEVGWYRPPFS-[cit]-VVHLY-amide
Immunoglobulin (Ig) superfamily protein expressed in the central nervous system capable of inducing MS like symptoms in animal models
Catalogue number crb1000345 Molecular Weight 2135.1 Sequence (one letter code) MEVGWYRPPFS-[cit]-VVHLY-amide Sequence (three letter code) H-Met-Glu-Val-Gly-Trp-Tyr-Arg-Pro-Pro-Phe-Ser-[cit]-Val-Val-His-Leu-Tyr-NH2. Molecular Weight 2135.1 Purity >95% References
Peschl et al (2017) Myelin Oligodendrocyte Glycoprotein: Deciphering a Target in Inflammatory Demyelinating Diseases. Front. Immunol. 8 529 PMID: 28533781
Raymond et al (2010) How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution. J. Immunol. 185(9) 5360 PMID: 20889553
Peschl et al (2017) Human antibodies against the myelin oligodendrocyte glycoprotein can cause complement-dependent demyelination. J. Neuroinflammation 14(1) 208 PMID: 29070051
Myelin oligodendrocyte glycoprotein (MOG) is a member of the immunoglobulin (Ig) protein superfamily and is expressed exclusively in the central nervous system (CNS) on the surface of myelin sheaths and oligodendrocyte processes. MOG is expressed at the onset of myelination, and therefore is a potential marker for oligodendrocyte maturation.
MOG contains an extracellular domain, a transmembrane domain, a cytoplasmic loop, a membrane-associated region and a cytoplasmic tail. MOG may function as a cell surface receptor or cell adhesion molecule. Fifteen different alternatively spliced isoforms have been detected in humans. These are present either on the cell surface, the endoplasmic reticulum in the endocytic system, or in secreted form.
The secreted form of MOG may trigger autoimmunity if released into the cerebrospinal fluid and periphery. MOG is thought to be a key target for autoantibodies and cell-mediated immune responses in inflammatory demyelinating diseases such as multiple sclerosis (MS) and is therefore widely studied in this field.
Fragment (35-51) of the human MOG can be rapidly degraded by the serine protease CatG. Conversion of arginine 46 to citrulline in this peptide reduces the sensitivity of the citrullinated MOG 35–51 peptide to degradation. This peptide has an uncharged C-terminal amide