Recombinant Mouse MOG Protein, CF

Myelin oligodendrocyte glycoprotein (MOG) is 28 kDa single-pass transmembrane glycoprotein that is a member of the Ig superfamily (1-4). Mouse MOG is synthesized with a 28 amino acid (aa) signal sequence, a 128 aa extracellular domain (ECD) containing an Ig-like domain, a 21 aa transmembrane domain, and a 69 aa cytosolic fragment featuring a hydrophobic domain that associates with the cytoplasmic face of the plasma membrane. The ECD of mature mouse MOG shares 90% and 95% aa sequence identity with the ECD of human and rat MOG, respectively. 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 function as an adhesion molecule as well as a mediator of immune activation in the CNS (2, 9, 13).

• MOG Antibodies
• MOG ELISA Kits
• MOG Lysates
• MOG Proteins
• MOG Proteins and Enzymes