Bovine Myelin basic protein

Cat.No. : MBP-6950B
Product Overview : Bovine Myelinbasic protein, was highly Purified from bovinecentral nervous system tissue by method of Määttä et al.
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Species : Bovine
Source : Bovine Central Nervous System Tissue
Tag : Non
Description : MBP is a peripheralmembrane protein, and its interaction with lipids is generally believed to becritical for the formation and stability of the multilamellar myelin sheath.It has been identified as a Ca2+-calmodulin regulated agent foractin polymerization, tropomyosin and actomyosin function, tubulinstabilization, and clathrin assembley. MBP is generally considered to be theantigen responsible for autoimmunity in multiple sclerosis (MS) and it hasthe capability to induce experimental allergic encephalomyelitis (EAE). MBPis also an endogenous inhibitor of the high-affinity cannabinoid binding sitein the brain and a substrate for numerous protein kinases (MAPK,serine/threonine kinase, protein kinase C). MBP is also suggested to beinvolved in intracellular signalling and as cytoskeletal components.
Purity : ≥95% (SDS-PAGE; immunoblot)
Formulation : Lyophilized. Essentially salt-free.
Reconstitution : Reconstitute with distilled water.
Application : Substratefor various kinases including MAPK, PKA, calmodulin-dependent protein kinase,PKC and phosphorylase kinase. Raf1, MEK, and MEKK can also use MBP as asubstrate.
Storage : Stablefor at least 1 year when stored at +4°C. Reconstituted protein is stable forat least 6 months at -20°C and for at least 24 hours at +37°C in aqueoussolution.
Gene Name MBP myelin basic protein [ Bostaurus ]
Official Symbol MBP
Synonyms MBP;myelin basic protein; myelin A1 protein; microtubule-stabilizing protein; 20kDa microtubule-stabilizing protein
Gene ID 618684
mRNA Refseq NM_001206674
Protein Refseq NP_001193603
Chromosome Location 24q11-q13.2
Function structuralconstituent of myelin sheath

TRC40 can deliver short secretory proteins to the Sec61 translocon

Journal: Journal of Cell Science    PubMed ID: 22505607    Data: 2012/8/1

Authors: Nicholas Johnson, Fabio Vilardi, Stephen High

Article Snippet:Proteins were synthesised using nuclease treated or untreated rabbit reticulocyte lysate in the presence of [ 35 S]methionine for 15 minutes at 30°C as before.Proteins were synthesised using nuclease treated or untreated rabbit reticulocyte lysate in the presence of [ 35 S]methionine for 15 minutes at 30°C as before.. The reaction was treated with 1 mM puromycin, immediately split, and MBP (Creative BioMart) or MBP-WRBcc ( ) added to 10 μM.. The reaction was incubated for 10 minutes at 30°C prior to addition of microsomes.The reaction was incubated for 10 minutes at 30°C prior to addition of microsomes.

WRBcc inhibits ppcecA translocation. ( A ) Radiolabelled forms of ppcecA, Sec61β and Cytb5 were synthesised in vitro as before and the resulting reaction mixture then incubated with varying concentrations of MBP-WRBcc as indicated. Canine pancreatic microsomes were added to allow translocation/integration and membranes recovered by centrifugation. Rabiolabelled proteins were detected by phosphorimaging following SDS-PAGE. N-glycosylated forms are indicated and in each case the fully glycosylated forms have been quantified relative to the matched untreated sample. ( B ) Graphical representation of relative N-glycosylation of proteins in response to increasing concentrations of MBP-WRBcc. Results are means ± s.e.

WRBcc inhibits ppcecA translocation. ( A ) Radiolabelled forms of ppcecA, Sec61β and Cytb5 were synthesised in vitro as before and the resulting reaction mixture then incubated with varying concentrations of MBP-WRBcc as indicated. Canine pancreatic microsomes were added to allow translocation/integration and membranes recovered by centrifugation. Rabiolabelled proteins were detected by phosphorimaging following SDS-PAGE. N-glycosylated forms are indicated and in each case the fully glycosylated forms have been quantified relative to the matched untreated sample. ( B ) Graphical representation of relative N-glycosylation of proteins in response to increasing concentrations of MBP-WRBcc. Results are means ± s.e.

WRBcc inhibits the ER delivery of translocation-competent fractions of short secretory proteins. Translocation-competent fractions of ppcecA, apelin and statherin were each pooled. Equivalent portions of the pooled fractions were incubated with either 10 μM maltose binding protein (MBP) or 10 μM MBP-WRBcc prior to the addition of membranes. The membrane fraction was recovered and proteins visualised by phosphorimaging following SDS-PAGE. N-glycosylated forms are indicated and the doubly modified products have each been quantified relative to their matched MBP control sample (set to 100%). Results in graph are means ± s.e.

WRBcc inhibits the ER delivery of translocation-competent fractions of short secretory proteins. Translocation-competent fractions of ppcecA, apelin and statherin were each pooled. Equivalent portions of the pooled fractions were incubated with either 10 μM maltose binding protein (MBP) or 10 μM MBP-WRBcc prior to the addition of membranes. The membrane fraction was recovered and proteins visualised by phosphorimaging following SDS-PAGE. N-glycosylated forms are indicated and the doubly modified products have each been quantified relative to their matched MBP control sample (set to 100%). Results in graph are means ± s.e.

WRBcc inhibition is alleviated upon TRC40 immunodepletion. ( A ) Depletion of TRC40 was confirmed by immunoblotting. ( B ) Rabbit reticulocyte lysate was immunodepleted for TRC40 or subjected to a mock treatment. Treated lysates were then used as before for in vitro translations and post-translational translocation assays in the presence of 10 μM MBP-WRBcc. N-glycosylated forms are indicated and quantified (means ± s.e.) relative to their matched MBP control samples as before.

WRBcc inhibition is alleviated upon TRC40 immunodepletion. ( A ) Depletion of TRC40 was confirmed by immunoblotting. ( B ) Rabbit reticulocyte lysate was immunodepleted for TRC40 or subjected to a mock treatment. Treated lysates were then used as before for in vitro translations and post-translational translocation assays in the presence of 10 μM MBP-WRBcc. N-glycosylated forms are indicated and quantified (means ± s.e.) relative to their matched MBP control samples as before.

Not For Human Consumption!

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