MBP，脱磷酸化

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).

从牛脑中纯化并使用λ蛋白磷酸酶去磷酸化的髓磷脂碱性蛋白。 通过用1 mg/mL抗磷酸MBP免疫印迹1微克MBP，无法检测到内源性磷酸化。

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.

在使用MAP激酶2/Erk2（目录号14-173）的激酶测定中常规评估为底物

10mM MOPS（pH 7.0）、128mM MnCl2、641mM EDTA、1.134 μg无活性λ磷酸酶和0.05%叠氮化钠

在-20°C下可保存2年

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