Myelin oligodendrocyte glycoprotein (MOG), a member of the immunoglobulin superfamily, is expressed exclusively in central nervous system myelin. Recent studies suggest that MOG may function in the completion, compaction, and maintenance of myelin in the central nervous system.1 Even though MOG physiological function is not entirely understood, studies have correlated the immune response of MOG to autoimmune mediated demyelination in several species.2 MOG is able to induce encephalitogenic T cell response, autoantibody response, and produce relapsing-remitting neurological disease with an extensive plaque-like demyelination.3 The autoantibody response to MOG [anti-MOG protein and anti-MOG (35-55) peptide] has been seen in MS patients and EAE-induced mice. This phenomenon suggests that MOG may have an important role in the development of MS and EAE, an experimental in vivo animal model for MS.4,5

Rabbit anti-MOG (35-55) polyclonal antibody was raised against a synthetic peptide from the N-terminus corresponding to amino acids 35-55 of mouse and rat MOG. There is only one amino acid residue difference between the mouse/rat and human MOG (35-55) peptide. ELISA results show that Anti-MOG (35-55) cross-react with human. The antibodies were also evaluated by Western blot.

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