Murine Myelin Basic Protein C1 Isoform (MBP - S17C,T95E-UTC1)
This variant is untagged pseudophosphorylated (Thr 95 substituted by Glu) rmMBP variant, UTC1, where Ser17 was substituted by Cys.
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 pseudophosphorylated (Thr 95 substituted by Glu) rmMBP variant, UTC1, where Ser17 was substituted by Cys.
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: | S17C,T95E-UTC1, untagged pseudophosphorylated (T95E) murine myelin basic protein C1 isoform with S17C substitution |
| Alternative Name(s): | MBP - S17C,T95E-UTC1 |
| Accession ID: | P02686 |
| Source: | murine protein overexpressed in E. coli BL21(DE3)-RIP |
| Molecular Weight: | 18,400.52 |
| Amino Acid Sequence: | ASQKRPSQRS KYLATACTMD HARHGFLPRH RDTGILDSIG RFFSGDRGAP KRGSGKDSHT RTTHYGSLPQ KSQHGRTQDE NPVVHFFKNI VTPREPPPSQ GKGRGLSLSR FSWGAEGQKP GFGYGGRASD YKSAHKGFKG AYDAQGTLSK IFKLGGRDSR SGSPMARR |
| Fusion Tag(s): | Untagged |
| Purity: | >90 %, purified by IMAC followed by ion-exchange chromatography |
| Buffer: | 20mM Hepes, pH 7.4 |
| Tested Applications: | 2.5 uM for fluorescence, 4 uM for circular dichroic spectroscopy |
| Comments: | pI 10.86 |
| 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., 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.
- Vassall K.A., Jenkins A.D., Bamm V.V., Harauz G. Thermodynamic analysis of the disorder-to-α-helical transition of 18.5-kDa myelin basic protein reveals an equilibrium intermediate representing the most compact conformation. J Mol Biol. 427 (2015) 1977-92.
- Vassall K.A., Bamm V.V., Jenkins A.D., Velte C.J., Kattnig D.R., Boggs J.M., Hinderberger D., Harauz G. Substitutions mimicking deimination and phosphorylation of 18.5-kDa myelin basic protein exert local structural effects that subtly influence its global folding. Biochim Biophys Acta. 1858 (2016) 1262-77.
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