Myelin oligodendrocyte glycoprotein (MOG) is a transmembrane protein belonging to immunoglobulin superfamily. 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. 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. This makes MOG a potential target of cellular and humoral immune responses in inflammatory demyelinating diseases.

Myelin Oligodendrocyte Glycoprotein (MOG) is a member of the immunoglobulin superfamily and is expressed exclusively in 
central nervous system (CNS). Although MOG protein constitutes only 0.01-0.05% of the CNS myelin proteins, it was 
demonstrated that MOG protein is a crucial autoantigen for multiple sclerosis in humans and experimental autoimmune 
encephalomyelitis (EAE) in rodents and monkeys (1-5). 
The purified human rMOG is recommended for in vitro studies such as T cell and B cell responses, cytokine response, 
antigen presentation, Western blotting, and ELISA as well as for in vivo study such as EAE induction in mice and monkeys. 
The following dosages are recommended: 5-20 μg/ml for in vitro study and 50-100 μg per animal for in vivo study