Anti-MBP / Myelin Basic Protein, clone MBP/4276

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Myelin basic protein (MBP) is the second most abundant protein in central nervous system (CNS) myelin: it comprises 30% of the total protein and about 10% of the dry weight of myelin. It is the only structural protein found so far to be essential for formation of CNS myelin, and has been called the executive molecule of myelin . MBP can interact with a number of polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and negatively charged lipids, and acquires structure on binding to them. It may act as a membrane actin-binding protein, which might allow it to participate in transmission of extracellular signals to the cytoskeleton in oligodendrocytes and tight junctions in myelin. MBP may be applicable as a marker for oligodendrogliomas. Phosphorylation been shown to decrease its ability to aggregate lipid vesicles and consequently destabilising the compact structure ofmyelin, a destruction that has been observed in demyelinating diseases such as Multiple Sclerosis. MBP/4276 is a useful detector of phosphorylated MBP by binding to Thr98 of human MBP in the phosphorylated state. Protein function: The classic group of MBP isoforms (isoform 4-isoform 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 (isoform 1-isoform 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 with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation. [The UniProt Consortium]