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Myelin oligodendrocyte glycoprotein (MOG) is a member of the immunoglobulin (Ig) protein superfamily and is expressed exclusively in the central nervous system 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 one extracellular domain, one transmembrane domain, one 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 triggering 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 and is therefore widely studied in this field.
The MOG (35-55) fragment is the most potent auto-antigenic region of MOG, and the most effective at inducing MS like symptoms in animal models. This peptide has a free carboxylic acid at the C-terminus
MOG(35-55) acid Mouse, Rat 0.5mg
MOG(35-55) acid Mouse, Rat 1mg
MOG(35-55) acid Mouse, Rat 5mg
MOG(35-55) acid Mouse, Rat 10mg
MOG(35-55) acid Mouse, Rat 25mg
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