Myelin basic protein is reported to account for about 30 of the proteins in myelin found in the central nervous system. It can induce experimental allergic encephalomyelitis (EAE), a T-lymphocyte mediated disease due to delayed-type hypersensitivity; though each animal species appears to respond to a different fragment of the 170 amino acid polypeptide. Four different isoforms have been identified through cDNA cloning. All four of these variants are identical except for the insertion or deletion of two peptide fragments encoded by exons 2 and 5. Myelin basic protein is reported to be expressed in oligodendrocytes, myelin of white matter in the brain and spinal cord and in peripheral nerves, though it is expressed less abundantly in gray matter.
MBP has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. In vitro, MBP is suitable as a substrate for numerous protein kinases, including the ERK and p38 MAP kinases that phosphorylate MBP at T98.
Note: This antibody detects in vitro-phosphorylated MBP of 21 kDa using Western blot. Based on sequence homology of the immunogen, this antibody should react with phosphorylated MBP from most common vertebrate species, including human, mouse, rat, and bovine.
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