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Sigma-Aldrich

MBP (myelin basic protein), bovine, purified

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UNSPSC Code:
12352200
eCl@ss:
32160405
NACRES:
NA.41

biological source

bovine

Quality Level

form

liquid

manufacturer/tradename

Upstate®

technique(s)

activity assay: suitable

UniProt accession no.

shipped in

wet ice

General description

Myelin basic protein (MBP) belongs to the intrinsically disordered protein family. It is localized in the insulating layer of nerve cells in the brain and spinal cord. It is an abundant protein found in the central nervous system (CNS).

Application

MBP (myelin basic protein), bovine, purified has been used in western blotting and as a standard in enzyme-linked immunosorbent assay (ELISA).

Biochem/physiol Actions

Myelin basic protein (MBP), known as the ‘executive molecule of myelin′, helps in the formation of central nervous system (CNS) myelin. Elevated levels of MBP in the cerebrospinal fluid (CSF) are detected in acute neurological disorders like exacerbating multiple sclerosis, and traumatic brain injury. It is also observed at increased levels during chronic progressive disorders including dementia, tumor cerebri, and metabolic disorders. 

Quality

routinely evaluated by successfully phosphorylating MAP Kinase 2/Erk2, active (Catalog # 14-173)

Physical form

10mM MOPS, pH 7.0, with 0.05% sodium azide

Storage and Stability

2 years at -20°C

Other Notes

This product is derived from bovine source. Export of this product to certain countries may be restricted. Please contact Customer Service or your local distributor to inquire about product availability and export options.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Tuoping Luo et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(8), 2860-2865 (2012-02-11)
Approximately 30% of human cancers harbor oncogenic gain-of-function mutations in KRAS. Despite interest in KRAS as a therapeutic target, direct blockade of KRAS function with small molecules has yet to be demonstrated. Based on experiments that lower mRNA levels of
Dajun Sang et al.
eLife, 8 (2019-08-14)
Protein kinases are crucial to coordinate cellular decisions and therefore their activities are strictly regulated. Previously we used ancestral reconstruction to determine how CMGC group kinase specificity evolved (Howard et al., 2014). In the present study, we reconstructed ancestral kinases
A C Maroney et al.
The Journal of biological chemistry, 276(27), 25302-25308 (2001-04-28)
CEP-1347 (KT7515) promotes neuronal survival at dosages that inhibit activation of the c-Jun amino-terminal kinases (JNKs) in primary embryonic cultures and differentiated PC12 cells after trophic withdrawal and in mice treated with 1-methyl-4-phenyl tetrahydropyridine. In an effort to identify molecular
Hung-Ming Lam et al.
Molecular and cellular endocrinology, 358(1), 27-35 (2012-03-01)
Multiple phosphorylation sites on the human estrogen receptor (hER)α were identified and shown to influence mammary carcinogenesis. In contrast, functional phosphorylation sites of hERβ have yet to be experimentally identified and validated. Here, using mass spectrometry, we uncovered three serines
S L Sutor et al.
The Journal of biological chemistry, 274(11), 7002-7010 (1999-03-06)
Cytokines trigger the rapid assembly of multimolecular signaling complexes that direct the activation of downstream protein kinase cascades. Two protein kinases that have been linked to growth factor-regulated proliferation and survival are mitogen-activated protein/ERK kinase (MEK) and its downstream target

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