Alpha Synuclein S87N Mutant Pre-formed Fibrils
SKU: BTL-SM-P-00242 |
Brand: Stressmarq
Product Description
| Cat Number | SPR-500E |
|---|---|
| Category | Recombinant Protein |
| Pack Size | 100 µg x5 |
| Description | Human Recombinant Alpha Synuclein S87N Mutant Pre-formed Fibrils |
| Applications | WB | In vivo Assay | 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 endogenous mouse α-syn pathology (1). A53T or S87N substitutions in human α-syn substantially accelerate fibrilization rates in vitro (2,3). Chimeric HuS87N fibrils show enhanced induction of α-syn pathology greater than both HuWT and MsWT fibrils in mice neuron cultures (4). Therefore, HuS87N is a good construct for inducing robust endogenous α-syn seeding and pathology in wild-type mice/cultures. |
| 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 |
Share Item: