Murine Myelin Basic Protein C8 Charge Isoform (MBP - UTC8)

This variant is untagged pseudodeiminated rmMBP variant, UTC8, where five Arg and one Lys were substituted by Gln.

The intrinsically disordered, 18.5-kDa isoform of Myelin Basic Protein (MBP) is a peripheral membrane protein that is essential to proper myelin formation in the central nervous system. Unmodified MBP (C1 charge variant, the most abundant variant of the healthy human adult myelin) is an extremely positively charged protein (+19 at neutral pH). MBP acts in oligodendrocytes both to adjoin membrane leaflets to each other in forming compact myelin sheath and as a hub in numerous protein-protein and protein-membrane interaction networks. Interaction of MBP with its various partners may be mediated, in part, by post-translation modifications (PTMs) such as phosphorylation and deimination that result in charge reduction and are developmentally regulated. Distinct patterns of post-translational modifications, most notably excessive deimination, also occur in multiple sclerosis, leading to speculation that these aberrant PTMs are a part of the disease pathogenesis.

From the laboratory of Scott D. Ryan, PhD, University of Guelph.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EGP010
Murine Myelin Basic Protein C8 Charge Isoform (MBP - UTC8)
0.5mg Limited stock
Regular Price:$580.00
On Sale:
Specifications

Product Type: Protein
Name: UTC8, Untagged recombinant murine myelin basic protein, C8 isoform
Alternative Name(s): MBP - UTC8
Accession ID: P02686
Source: murine protein overexpressed in E. coli BL21(DE3)-RIP
Molecular Weight: 18,216.13
Amino Acid Sequence: ASQKRPSQRS KYLATASTMD HAQHGFLPRH QDTGILDSIG RFFSGDRGAP KRGSGKDSHT RTTHYGSLPQ KSQHGRTQDE NPVVHFFKNI VTPRTPPPSQ GKGRGLSLSR FSWGAEGQQP GFGYGGQASD YKSAHKGFKG AYDAQGTLSK IFKLGGQDSR SGSPMARQ
Fusion Tag(s): Untagged
Purity: >90 %, purified by IMAC followed by ion-exchange chromatography
Buffer: 10mM KPB pH 7.4
Comments: pI 10.46
Storage: -80C
Shipped: Dry Ice

Provider
From the laboratory of Scott D. Ryan, PhD, University of Guelph.
References
  1. K.A. Vassall, V.V. Bamm, G. Harauz, MyelStones: the executive roles ofmyelin basic protein in myelin assembly and destabilization in multiple sclerosis, Biochem. J. 472 (2015) 17Ð32.
  2. Bamm, V. V., M. A. Ahmed, and G. Harauz. Interaction of myelin basic protein with actin in the presence of dodecyl phosphocho- line micelles. Biochemistry. 49 (2010) 6903Ð6915.
  3. Smith G.S., Chen L, Bamm V.V., Dutcher J.R., Harauz G. The interaction of zinc with membrane-associated 18.5 kDa myelin basic protein: an attenuated total reflectance-Fourier transform infrared spectroscopic study. Amino Acids. 39 (2010) 739-750.
  4. Ahmed M.A., Bamm V.V., Harauz G., Ladizhansky V. Solid-state NMR spectroscopy of membrane-associated myelin basic protein--conformation and dynamics of an immunodominant epitope. Biophys J. 99 (2010) 1247-55.

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