M1891
Myelin Basic Protein bovine
≥90% (SDS-PAGE), lyophilized powder, suitable for activity assay
Synonym(s):
MBP
Product Name
Myelin Basic Protein bovine, ≥90% (SDS-PAGE), lyophilized powder, suitable for activity assay
biological source
bovine
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
Quality Level
Gene Information
cow ... MBP(618684)
Analysis Note
May contain traces of urea-glycine buffer salts.
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.
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.
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
监管及禁止进口产品
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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)
Vebjørn Martinsen et al.
Amino acids, 54(1), 99-109 (2021-12-11)
Myelin basic protein (MBP) is an abundant protein in central nervous system (CNS) myelin. MBP has long been studied as a factor in the pathogenesis of the autoimmune neurodegenerative disease multiple sclerosis (MS). MS is characterized by CNS inflammation, demyelination
Functional characterization of a mitochondrial Ser/Thr protein phosphatase in cell death regulation.
Lu G
Methods in Enzymology, 457, 255-273 (2009)
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)
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