MOG (34-56) Human amide GMEVGWYRPPFSRVVHLYRNGKD-amide
Immunoglobulin (Ig) superfamily protein expressed in the central nervous system capable of inducing MS like symptoms in animal models
Catalogue number crb1000240 Molecular Weight 2763.14 Sequence (one letter code) GMEVGWYRPPFSRVVHLYRNGKD-amide Sequence (three letter code)
Purity >95% Storage -20°C References
Araman et al (2019) Amyloid-like Behavior of Site-Specifically Citrullinated Myelin Oligodendrocyte Protein (MOG) Peptide Fragments inside EBV-Infected B-Cells Influences Their Cytotoxicity and Autoimmunogenicity. Biochem. PMID: 30513201
Peschl et al (2017) Myelin Oligodendrocyte Glycoprotein: Deciphering a Target in Inflammatory Demyelinating Diseases. Front. Immunol. 8 529 PMID: 28533781
Weber et al (2018) Defining distinct features of anti-MOG antibody associated central nervous system demyelination. Ther. Adv. Neurol. Disord. 11 175628641876208. PMID: 29623106.
Peschl et al (2017) Human antibodies against the myelin oligodendrocyte glycoprotein can cause complement-dependent demyelination. J. Neuroinflammation, 14(1) 208 PMID: 29070051
Manufactured in: United Kingdom
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.
The MOG (34-56) fragment is in the most potent auto-antigenic region of MOG, and is highly effective at inducing experimental autoimmune/allergic encephalomyelitis (EAE), an animal model that resembles MS. This peptide has an uncharged C-terminal amide