Product Description
| Cat Number | SPR-499XE |
|---|---|
| Category | Recombinant Protein |
| Pack Size | 500 µg (@5mg/ml) |
| Description | Human Recombinant Alpha Synuclein S87N Mutant Monomers |
| Applications | WB | SDS PAGE | In vitro Assay |
| Target | Alpha Synuclein S87N Mutant |
| Molecular Weight | 14.46 kDa |
| Purity | >95% |
| Research Area | Neuroscience | Neurodegeneration | Alzheimer's Disease | Tangles & Tau | Neuroscience | Neurodegeneration | Parkinson's Disease | Synuclein | Neuroscience | Neurodegeneration | Multiple System Atrophy |
| Swiss Prot | P37840-1 |
| Scientific Background | Human alpha synuclein S87N mutant (HuS87N) has Ser87 mutated to the equivalent mouse residue Asn87, effectively making it a human-mouse chimeric protein. Despite sequence differences at only seven residues, or 5% of the total 140 amino acids, the aggregation rate of wild-type mouse α-syn (MsWT) is faster than wild-type human α-syn (HuWT) in vitro. In wild-type mouse models, MsWT fibrils are more efficient than HuWT fibrils at inducing pathology of endogenous mouse α-syn (1). A53T or S87N substitutions in human α-syn substantially accelerate fibrilization rates in vitro (2,3). Chimeric HuS87N fibrils show enhanced pathogenicity to wild-type mouse neurons, greater than HuWT, HuA53T, and MsWT fibrils (4). HuS87N fibrils can be used as a more human-like alternative to MsWT fibrils to induce equivalent or greater endogenous α-syn seeding and pathology in wild-type mice. |
| Expression System | E. coli |
| Accession Number | NP_000336.1 |
| Gene Id | 6622 |
| Protein Length | 140 AA |
| Amino Acid Sequence | MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA |
| Purification | Ion-exchange Purified |
| Storage | -80ºC |
| References | 1. Masuda-Suzukake et al. 2013. Prion-like Spreading of Pathological α-synuclein in Brain. Brain. https://doi.org/10.1093/brain/awt037 2. Kang, K. et al. 2011. The A53T Mutation is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse α-synuclein. JACS. https://doi.org/10.1021/ja203979j 3. Ohgita, T. et al. 2023. Intramolecular Interaction Kinetically Regulates Fibril Formation by Human and Mouse Alpha-Synuclein. Sci Rep https://doi.org/10.1038/s41598-023-38070-4 4. Luk, K., C. et al. 2016. Molecular and Biological Compatibility with Host Alpha-Synuclein Influences Fibril Pathogenicity. Cell Rep. https://doi.org/10.1016/j.celrep.2016.08.053 |
| Product Url | View Document |
| Note | The product is for research use only |
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