Murine Myelin Basic Protein C1 Isoform (MBP - UTC1)
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.
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.
| Product Type: | Protein |
| Name: | UTC1, Recombinant murine myelin basic protein C1 isoform, no tags |
| Alternative Name(s): | MBP - UTC1 |
| Accession ID: | P02686 |
| Source: | murine protein overexpressed in E. coli BL21(DE3)-RIP |
| Molecular Weight: | 18,356.45 |
| Amino Acid Sequence: | ASQKRPSQRS KYLATASTMD HARHGFLPRH RDTGILDSIG RFFSGDRGAP KRGSGKDSHT RTTHYGSLPQ KSQHGRTQDE NPVVHFFKNI VTPRTPPPSQ GKGRGLSLSR FSWGAEGQKP GFGYGGRASD YKSAHKGFKG AYDAQGTLSK IFKLGGRDSR SGSPMARR |
| Fusion Tag(s): | Untagged |
| Purity: | >90 %, purified by IMAC followed by ion-exchange chromatography |
| Buffer: | 10mM KPB pH 7.4 |
| Comments: | pI 11.14 |
| Storage: | -80C |
| Shipped: | Dry Ice |
- 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.
- 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.
- 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.
- 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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