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Key Documents

13-110

Sigma-Aldrich

MBP, Dephosphorylated

Synonym(s):

MBP protein

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About This Item

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

biological source

bovine

Quality Level

form

liquid

shelf life

2 yr

manufacturer/tradename

Upstate®

technique(s)

activity assay: suitable

solubility

water: soluble

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

bovine ... MBP(618684)

General description

Research Area: Cell Signaling
Myelin basic protein (MBP) constitutes approximately 30% of the total protein and accounts for about 10% of the dry weight of myelin. It is primarily associated with the cytosolic side of the oligodendrocyte (OL) membrane, largely through electrostatic interactions with acidic lipids. This protein is distributed throughout compact internodal myelin. MBP consists of multiple post-translationally modified isomers with varying charges, some of which arise from phosphorylation at several sites by different kinases, including mitogen-activated protein kinase (MAPK).

Application

Myelin basic protein purified from bovine brain and de-phosphorylated using Lambda protein phosphatase. No detectable endogenous phosphorylation as determined by immunoblotting 1 microgram of MBP with 1 microgram/ml anti phospho MBP.

Biochem/physiol Actions

Myelin basic protein (MBP) is distributed throughout compact internodal myelin. It binds to negatively charged lipids on the cytosolic surface of oligodendrocyte membranes, likely facilitating the adhesion of these surfaces in the multilayered myelin sheath. MBP is characterized as an intrinsically unstructured protein, providing it with the flexibility to bind to a charged surface along its entire length and adapt its local conformation as needed to optimize binding to various targets. Such proteins often function as multifunctional regulatory proteins.
MBP interacts with polyanions such as actin filaments and microtubules in vitro and binds to other ligands such as Ca2+-calmodulin (CaM). MBP binds to G-actin, inducing its polymerization, and it bundles actin filaments. It also polymerizes actin, bundles F-actin filaments, and binds actin filaments to lipid bilayers through electrostatic interactions. Phosphorylation and dephosphorylation of MBP occur in the myelin sheath in response to electrical activity in the brain.

Quality

routinely evaluated as a substrate in a kinase assay using MAP Kinase 2/Erk2 (Catalog # 14-173)

Physical form

10mM MOPS, pH 7.0, 128mM MnCl2, 641mM EDTA, 1.134μg inactive lambda phosphatase and 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.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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Gaëlle Lentini et al.
Nature communications, 12(1), 3788-3788 (2021-06-20)
Active host cell invasion by the obligate intracellular apicomplexan parasites relies on the formation of a moving junction, which connects parasite and host cell plasma membranes during entry. Invading Toxoplasma gondii tachyzoites secrete their rhoptry content and insert a complex
J W Crabb et al.
Protein science : a publication of the Protein Society, 7(3), 746-757 (1998-04-16)
Cellular retinaldehyde-binding protein (CRALBP) is abundant in the retinal pigment epithelium (RPE) and Müller cells of the retina where it is thought to function in retinoid metabolism and visual pigment regeneration. The protein carries 11-cis-retinal and/or 11-cis-retinol as endogenous ligands
Thrombospondin stimulates focal adhesion disassembly through Gi- and phosphoinositide 3-kinase-dependent ERK activation
Orr, A. W., et al
The Journal of Biological Chemistry, 277, 20453-20460 (2002)
Cyclic AMP decreases the phosphorylation state of myelin basic proteins in rat brain cell cultures.
Ulmer, J B, et al.
The Journal of Biological Chemistry, 262, 1748-1755 (1987)
D L Lefebvre et al.
The Biochemical journal, 355(Pt 2), 297-305 (2001-04-04)
Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK)

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