Human α-Synuclein, A53T Variant (α-syn-A53T)
Alpha-synuclein A53T variant.
Alpha-synuclein (α-synuclein) is an intrinsically disordered protein of unknown function that is linked to both familial and sporadic cases of Parkinson's disease, where it forms the major constituent of the pathological Lewy body aggregates. Certain cases of early-onset familial Parkinson's disease have been connected to the A53T α-synuclein variant; therefore, this peptide can be used for binding studies as well as for modelling Parkinson's via the generation of fibrils, which have been shown to seed endogenous α-synuclein inclusions in healthy cells.
From the laboratory of Scott D. Ryan, PhD, University of Guelph.
Alpha-synuclein A53T variant.
Alpha-synuclein (α-synuclein) is an intrinsically disordered protein of unknown function that is linked to both familial and sporadic cases of Parkinson's disease, where it forms the major constituent of the pathological Lewy body aggregates. Certain cases of early-onset familial Parkinson's disease have been connected to the A53T α-synuclein variant; therefore, this peptide can be used for binding studies as well as for modelling Parkinson's via the generation of fibrils, which have been shown to seed endogenous α-synuclein inclusions in healthy cells.
From the laboratory of Scott D. Ryan, PhD, University of Guelph.
Specifications
| Product Type: | Protein |
| Name: | recombinant human _-synuclein mutant A53T variant |
| Alternative Name(s): | alpha-syn-A53T |
| Accession ID: | P37840 |
| Source: | Human, expressed in E. coli BL21 (DE3) CP+ |
| Molecular Weight: | 14,490.10 |
| Amino Acid Sequence: | MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP |
| Fusion Tag(s): | None |
| Purity: | >95 %, purified by ion-exchange chromatography followed by reverse phase chromatography |
| Buffer: | 10mM KPB pH 7.4 |
| Storage: | -80C |
| Shipped: | Dry Ice |
Provider
From the laboratory of Scott D. Ryan, PhD, University of Guelph.
References
- Ryan, T., Bamm, V.V., Stykel, M.G., Coackley, C.L., Humphries, K.M., Jamieson-Williams, R., Ambasudhan, R., Mosser, D.D., Lipton, S.A., Harauz, G., et al. (2018). Cardiolipin exposure on the outer mitochondrial membrane modulates α-synuclein. Nat. Commun 9, 1-17. doi:10.1038/s41467-018-03241-9.
- Stykel, M.G., Humphries, K., Kirby, M.P., Czaniecki, C., Wang, T., Ryan, T., Bamm, V., Ryan, S.D. (2018). Nitration of microtubules blocks axonal mitochondrial transport in a human pluripotent stem cell model of Parkinsons disease. Faseb. J 32, 5350-5364. doi:10.1096/fj.201700759RR.
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