Murine Myelin Basic Protein, S133-S159, Calmodulin Binding Domain (MBP a3- peptide)
This variant is untagged C-terminal peptide (S133-S159) of murine MBP variant, C1. This peptide is an amphipathicΑ-helix and comprises the primary calmodulin-binding domain in the MBP sequence.
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 untagged C-terminal peptide (S133-S159) of murine MBP variant, C1. This peptide is an amphipathicΑ-helix and comprises the primary calmodulin-binding domain in the MBP sequence.
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: | alpha 3 C-terminal MBP peptide, untagged S133-S159 peptide of murine myelin basic protein C1 isoform |
| Alternative Name(s): | MBP a3- peptide |
| Accession ID: | P02686 |
| Source: | SUMO-fused murine peptide overexpressed in E. coli BL21(DE3)-RIP |
| Molecular Weight: | 2,840.19 |
| Amino Acid Sequence: | SAHKGFKG AYDAQGTLSK IFKLGGRDS |
| 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 9.82 |
| 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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