Myelin basic protein [26]

GWB-E2245F

IgG1

Human

Tissue culture supernatant Storage

For IHC-Fr: Use at an assay dependent dilution. Not tested in other applications. Optimal dilutions/concentrations should be determined by the researcher. The classic group of Myelin basic protein (MBP) isoforms (isoforms 4-14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoforms 1-3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination maybe as components of transcriptional complexes and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined to optional posttranslational modifications give a wide spectrum of isomers each of them having maybe a specialized function.

Homodimer; isoform 3 exists as a homodimer.

MBP isoforms are found in both the central and the peripheral nervous system whereas Golli-MBP isoforms are expressed in fetal thymus spleen and spinal cord as well as in cell lines derived from the immune system. Developmental Stage: Expression begins abruptly in 14-16 week old fetuses. Even smaller isoforms seem to be produced during embryogenesis; some of these persisting in the adult. Expression of isoform MBP2 is more evident at 16 weeks and its relative proportion declines thereafter.

The N-terminal alanine is acetylated (isoform 3 isoform 4 isoform 5 and isoform 6).

The reduction in the surface charge of citrullinated and/or methylated MBP could result in a weakened attachment to the myelin membrane. This mechanism could be operative in demyelinating diseases such as chronical multiple sclerosis (MS) and fulminating MS (Marburg disease).