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MBP recombinant protein :: Myelin basic protein Recombinant Protein

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Catalog # MBS717422
Unit / Price
  0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
SDS-Page
Product Name

Myelin basic protein (MBP), Recombinant Protein

Also Known As

Recombinant Human Myelin basic protein

Product Synonym Names
Myelin A1 protein; Myelin membrane encephalitogenic protein
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
134-304
Sequence Length
197
Sequence
MASQKRPSQR HGSKYLATAS TMDHARHGFL PRHRDTGILD SIGRFFGGDR GAPKRGSGKV PWLKPGRSPL PSHARSQPGL CNMYKDSHHP ARTAHYGSLP QKSHGRTQDE NPVVHFFKNI VTPRTPPPSQ GKGRGLSLSR FSWGAEGQRP GFGYGGRASD YKSAHKGFKG VDAQGTLSKI FKLGGRDSRS GSPMARR
OMIM
159430
3D Structure
ModBase 3D Structure for P02686
Host
E Coli
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of MBP recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
MBP recombinant protein
The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in ryelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of th potentially having a specialized function. Induces T-cell proliferation.
Product Categories/Family for MBP recombinant protein

MBP recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for MBP. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
25.6kD
NCBI Official Full Name
myelin basic protein isoform 1
NCBI Official Synonym Full Names
myelin basic protein
NCBI Official Symbol
NCBI Protein Information
Golli-MBP; myelin basic protein
UniProt Protein Name
Myelin basic protein
UniProt Synonym Protein Names
Myelin A1 protein; Myelin membrane encephalitogenic protein
Protein Family
UniProt Gene Name
UniProt Synonym Gene Names
UniProt Entry Name
MBP_HUMAN
NCBI Summary for MBP
The protein encoded by the classic MBP gene is a major constituent of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system. However, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs arise from the long MBP gene (otherwise called "Golli-MBP") that contains 3 additional exons located upstream of the classic MBP exons. Alternative splicing from the Golli and the MBP transcription start sites gives rise to 2 sets of MBP-related transcripts and gene products. The Golli mRNAs contain 3 exons unique to Golli-MBP, spliced in-frame to 1 or more MBP exons. They encode hybrid proteins that have N-terminal Golli aa sequence linked to MBP aa sequence. The second family of transcripts contain only MBP exons and produce the well characterized myelin basic proteins. This complex gene structure is conserved among species suggesting that the MBP transcription unit is an integral part of the Golli transcription unit and that this arrangement is important for the function and/or regulation of these genes. [provided by RefSeq, Jul 2008]
UniProt Comments for MBP
The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation.
Product References and Citations for MBP recombinant protein
Amino acid sequence of the encephalitogenic basic protein from human myelin.Carnegie P.R.Biochem. J. 123:57-67(1971) Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant.Roth H.J., Kronquist K.E., Pretorius P.J., Crandall B.F., Campagnoni A.T.J. Neurosci. Res. 16:227-238(1986) Identification of three forms of human myelin basic protein by cDNA cloning.Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986) Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning.Roth H.J., Kronquist K.E., de Rosbo N., Crandall B.F., Campagnoni A.T.J. Neurosci. Res. 17:321-328(1987) The organization of the human myelin basic protein gene. Comparison with the mouse gene.Streicher R., Stoffel W.Biol. Chem. Hoppe-Seyler 370:503-510(1989) The human myelin basic protein gene is included within a 179-kilobase transcription unit expression in the immune and central nervous systems.Pribyl T.M., Campagnoni C.W., Kampf K., Kashima T., Handley V.W., McMahon J., Campagnoni A.T.Proc. Natl. Acad. Sci. U.S.A. 90:10695-10699(1993) Purification of immunologically active recombinant 21.5 kDa isoform of human myelin basic protein.Nye S.H., Pelfrey C.M., Burkwit J.J., Voskuhl R.R., Lenardo M.J., Mueller J.P.Mol. Immunol. 32:1131-1141(1995) Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis. JNK-and caspase-dependent nuclear localization is a requirement for membrane blebbing.Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D.J. Biol. Chem. 282:6484-6493(2007) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal.Smith G.S., Seymour L.V., Boggs J.M., Harauz G.Biochem. Biophys. Res. Commun. 422:670-675(2012) Identification and Characterization of citrulline-modified brain proteins by combining HCD and CID fragmentation.Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.Proteomics 13:2682-2691(2013) Conformation of a tetradecapeptide epitope of myelin basic protein.Mendz G.L., Barden J.A., Martenson R.E.Eur. J. Biochem. 231:659-666(1995) Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis.Ridsdale R.A., Beniac D.R., Tompkins T.A., Moscarello M.A., Harauz G.J. Biol. Chem. 272:4269-4275(1997) Structural basis for the binding of an immunodominant peptide from myelin basic protein in different registers by two HLA-DR2 proteins.Li Y., Li H., Martin R., Mariuzza R.A.J. Mol. Biol. 304:177-188(2000) Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II.Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P., Schlievert P.M., Mariuzza R.A.Immunity 14:93-104(2001) Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule.Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.EMBO J. 24:2968-2979(2005)

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