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M1891

Sigma-Aldrich

Myelin Basic Protein bovine

≥90% (SDS-PAGE), lyophilized powder, suitable for activity assay

Synonym(s):

MBP

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

bovine

Quality Level

Assay

≥90% (SDS-PAGE)

form

lyophilized powder

mol wt

18.4 kDa

storage condition

(Keep container tightly closed in a dry and well-ventilated place)

technique(s)

activity assay: suitable

solubility

water: 1 mg/mL, clear, colorless to faintly yellow

UniProt accession no.

storage temp.

−20°C

Gene Information

cow ... MBP(618684)

General description

Research Area: Cell Signaling

Myelin basic protein (MBP), a single-chain polypeptide consisting of 170 amino acids with a methyl-arginine, is a peripheral membrane protein. This crucial structural component of the myelin sheath is the second-most abundant protein in myelin representing about 30% of the total myelin protein.

Application

Myelin Basic Protein (MBP) bovine has been used:

  • in in vitro methylation reaction
  • as a substrate in in vitro immunoprecipitation-kinase assay to measure Cds1 (the S-phase-specific checkpoint effector kinase) activity
  • to prepare phosphorylated MBP, which is used as a substrate in phosphatase assays
Used as a kinase substrate.

Biochem/physiol Actions

Mutation of the myelin basic protein gene induces dysmyelination. It is used to induce experimental allergic encephalomyelitis.
Myelin basic protein (MBP) plays a vital role in the formation of the myelin sheath and is associated with various neurological disorders. MBP functions as an antigenic target in the autoimmune disease experimental allergic encephalomyelitis (EAE). MBP plays an essential role in cytoskeletal turnover and membrane extension. Additionally, it is also involved in Fyn-mediated signaling pathways, sequestration of phosphoinositide, and regulation of calcium homoeostasis. MBP functions as an in vitro substrate for mitogen-activated protein kinase (MAP) kinase and aids in the purification and functional studies of enzymes.MBP serves as a potential neuroreceptor. It can stimulate the proliferation of lymphocytes in vitro. MBP plays a key role as a substrate in the mitogen-activated protein (MAP) kinase activation pathway. Based on lymphocyte stimulation, MBP can be used to detect cancer. It is used in several immunological studies. MBP also contributes to the preservation of the lipid: protein organization within myelin.

Quality

May contain traces of urea-glycine buffer salts.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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The lateral membrane organization and dynamics of myelin proteins PLP and MBP are dictated by distinct galactolipids and the extracellular matrix
Ozgen H, et al.
PLoS ONE (2014)
Michal Jasinski et al.
Plant physiology, 147(2), 719-731 (2008-04-09)
The analysis of gene expression in Arabidopsis (Arabidopsis thaliana) using cDNA microarrays and reverse transcription-polymerase chain reaction showed that AtOSA1 (A. thaliana oxidative stress-related Abc1-like protein) transcript levels are influenced by Cd2+ treatment. The comparison of protein sequences revealed that
Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast.
Sayegh J and Clarke SG
Biochemical and Biophysical Research Communications, 372(4), 811-815 (2008)
C Delehouzé et al.
Scientific reports, 7(1), 12931-12931 (2017-10-12)
Necroptosis is a programmed cell death pathway that has been shown to be of central pathophysiological relevance in multiple disorders (hepatitis, brain and cardiac ischemia, pancreatitis, viral infection and inflammatory diseases). Necroptosis is driven by two serine threonine kinases, RIPK1
Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain.
Sayegh J
The Journal of Biological Chemistry, 282(50), 36444-36453 (2007)

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