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Myelin Basic Protein, Bovine (MBP)

Cat no: M9758


Supplier: United States Biological
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In vitro, myelin basic protein (MBP) is a substrate for phosphorylation by several different protein kinases including MAPK, PKA, calmodulin-dependent protein kinase, PKC and phosphorylase kinase. Even highly specific protein kinases such as Raf1, MEK and MEKK can utilize MBP as an alternative substrate. Myelin basic protein (MBP) is a single-chain, flexible polypeptide of about 18.5kD existing in its natural environment as an extrinsic and loosely bound component of the cytoplasmic portion of the myelin membrane sandwich. Ultrastructural immunocytochemistry with anti-myelin basic protein has shown that MBP is localized in the compact myelin sheath. MBP has not been demonstrated in rough endoplasmic reticulum, lysosomes or any other cytoplasmic organelles. MBP serves as a marker for oligodendrocytes and Schwann cells. MBP is also a marker for malignant schwannomas and appears to play a significant role in the etiology of multiple sclerosis and experimental autoimmune encephalomyelitis. Note: Supplied as 4 vials of 2.5mg each in 500ul buffer or as 1x10mg. Applications: Protein Kinase Assay: This lot was successfully phosphorylated using M2362-06 MAPK 2/Erk2, active in a kinase assay. Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: M9758
Size: 10mg
Form: Supplied as a liquid in 10mM MOPS, pH 7.0, 0.05% sodium azide.
Purity: (same/more than) 95% (SDS-PAGE and Coomassie blue staining)
References: 1. Cicirelli, et al., J. Biol. Chem. 263: 2009, 1988. 2. Martenson, et al., J. Biol. Chem. 258: 930, 1983. 3. Ulmer, et al., J. Biol. Chem. 262: 1748, 1987. 4. Diebler, G.E., Preparative Biochemistry 2(2): 139-165 (1972).

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