Myelin Basic Protein >90% Pure (MBP) Native Protein

The protein encoded by the classic Mbp gene is a major constituent of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system. However, Mbp-related transcripts are also present in the bone marrow and the immune system. These mRNAs arise from the long Mbp gene (otherwise called "Golli-Mbp") that contains 3 additional exons located upstream of the classic Mbp exons. Alternative splicing from the Golli and the Mbp transcription start sites gives rise to 2 sets of Mbp-related transcripts and gene products. The Golli mRNAs contain 3 exons unique to Golli-Mbp, spliced in-frame to 1 or more Mbp exons. They encode hybrid proteins that have N-terminal Golli aa sequence linked to Mbp aa sequence. The second family of transcripts contain only Mbp exons and produce the well characterized myelin basic proteins. This complex gene structure is conserved among species suggesting that the Mbp transcription unit is an integral part of the Golli transcription unit and that this arrangement is important for the function and/or regulation of these genes. Mutation of the Mbp gene is associated with the 'shiverer' and 'myelin deficient' phenotypes in mouse. [provided by RefSeq]

Function: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane

Subunit structure: Homodimer

Subcellular location: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic side of myelin.

Tissue specificity: Found in both the central and the peripheral nervous system.

Post-translational modification: As in other animals, several charge isomers may be produced as a result of optional post-translatonial modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues.Arg-131 was found to be 44% monomethylated and 11% symmetrically dimethylated.

Sequence similarities: Belongs to the myelin basic protein family.