13C,15N-Murine Myelin Basic Protein C1 Isoform, 1-105 (MBP 13C,15N-DC-rmMBP)
This variant is isotopically labeled with 13C and 15N, C-terminal deletion variant of recombinant murine myelin basic protein C1 isoform with glycine substituted by tryptophan at position 105, A1-G105W-6His, ΔC-rmMBP-C1
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.
This variant is isotopically labeled with 13C and 15N, C-terminal deletion variant of recombinant murine myelin basic protein C1 isoform with glycine substituted by tryptophan at position 105, A1-G105W-6His, ΔC-rmMBP-C1
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: | Delta-C-rmMBP-C1, isotopically labeled with 13C and 15N, C-terminal deletion variant of recombinant murine myelin basic protein C1 isoform, A1-G105W-6His |
| Alternative Name(s): | MBP 13C,15N-DC-rmMBP |
| Accession ID: | P02686 |
| Source: | murine protein overexpressed in E. coli BL21(DE3)-RIP |
| Molecular Weight: | 12,582.90 |
| Amino Acid Sequence: | ASQKRPSQRS KYLATASTMD HARHGFLPRH RDTGILDSIG RFFSGDRGAP KRGSGKDSHT RTTHYGSLPQ KSQHGRTQDE NPVVHFFKNI VTPRTPPPSQ GKGRWHHHHH H |
| Fusion Tag(s): | C-terminal tag: W HHHHHH |
| Purity: | >90 %, purified by IMAC followed by ion-exchange chromatography |
| Buffer: | 10mM KPB pH 7.4 |
| Comments: | pI 11.39 |
| 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.
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