13C,15N-Murine Myelin Basic Protein, S72-S107, Immuno-Dominant Epitope (MBP-13C,15N-a2-peptide)
This variant is isotopically labeled 13C, 15N untagged central peptide (S72-S107) of murine MBP variant, C1. This peptide is a highly conserved central segment of MBP, which comprises a membrane-anchoring amphipathic α-helix followed by a proline-rich segment that represents a ligand for SH3 domain-containing proteins. Also, this peptide contains the immono-dominant epitope involved in multiple sclerosis pathogenesis.
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 13C, 15N untagged central peptide (S72-S107) of murine MBP variant, C1. This peptide is a highly conserved central segment of MBP, which comprises a membrane-anchoring amphipathic α-helix followed by a proline-rich segment that represents a ligand for SH3 domain-containing proteins. Also, this peptide contains the immono-dominant epitope involved in multiple sclerosis pathogenesis.
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: | 13C, 15N -alpha 2 central MBP peptide, untagged S72-S107 peptide of murine myelin basic protein C1 isoform |
| Alternative Name(s): | MBP - 13C,15N-a2-peptide |
| Accession ID: | P02686 |
| Source: | SUMO-fused murine peptide overexpressed in E. coli BL21(DE3)-RIP |
| Molecular Weight: | 3,970.42 |
| Amino Acid Sequence: | SQHGRTQDEN PVVHFFKNIV TPRTPPPSQG KGRGLS |
| Fusion Tag(s): | Untagged |
| Purity: | >95 %, purified by IMAC of SUMO-fused peptide followed by cleavage of SUMO-tag and second IMAC. Finally purified by reverse-phase HPLC |
| Buffer: | 10mM KPB pH 7.4 |
| Tested Applications: | 4 uM for circular dichroic spectroscopy |
| Comments: | pI 10.9 |
| Storage: | -80C |
| Shipped: | Dry Ice |
- K.A. Vassall, V.V. Bamm, G. Harauz, MyelStones: the executive roles of myelin basic protein in myelin assembly and destabilization in multiple sclerosis, Biochem. J. 472 (2015) 17Ð32.
- Bamm V.V., De Avila M., Smith G.S., Ahmed M.A., Harauz G. Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction. Biophys J. 101 (2011) 1248-56.
- Ahmed M.A., De Avila M., Polverini E., Bessonov K., Bamm V.V., Harauz G. Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles. Biochemistry. 51 (2012) 7475-87.
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