MBP, Dephosphorylated

Research Area: Cell Signaling
Myelin basic protein (MBP) constitutes approximately 30% of the total protein and accounts for about 10% of the dry weight of myelin. It is primarily associated with the cytosolic side of the oligodendrocyte (OL) membrane, largely through electrostatic interactions with acidic lipids. This protein is distributed throughout compact internodal myelin. MBP consists of multiple post-translationally modified isomers with varying charges, some of which arise from phosphorylation at several sites by different kinases, including mitogen-activated protein kinase (MAPK).

Myelin basic protein purified from bovine brain and de-phosphorylated using Lambda protein phosphatase. No detectable endogenous phosphorylation as determined by immunoblotting 1 microgram of MBP with 1 microgram/ml anti phospho MBP.

Myelin basic protein (MBP) is distributed throughout compact internodal myelin. It binds to negatively charged lipids on the cytosolic surface of oligodendrocyte membranes, likely facilitating the adhesion of these surfaces in the multilayered myelin sheath. MBP is characterized as an intrinsically unstructured protein, providing it with the flexibility to bind to a charged surface along its entire length and adapt its local conformation as needed to optimize binding to various targets. Such proteins often function as multifunctional regulatory proteins.
MBP interacts with polyanions such as actin filaments and microtubules in vitro and binds to other ligands such as Ca²⁺-calmodulin (CaM). MBP binds to G-actin, inducing its polymerization, and it bundles actin filaments. It also polymerizes actin, bundles F-actin filaments, and binds actin filaments to lipid bilayers through electrostatic interactions. Phosphorylation and dephosphorylation of MBP occur in the myelin sheath in response to electrical activity in the brain.

routinely evaluated as a substrate in a kinase assay using MAP Kinase 2/Erk2 (Catalog # 14-173)

10mM MOPS, pH 7.0, 128mM MnCl2, 641mM EDTA, 1.134μg inactive lambda phosphatase and 0.05% sodium azide

2 years at -20°C

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