Alpha Synuclein S87N Mutant Monomers

Alpha Synuclein S87N Mutant Monomers

• 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.
• Description: Human Recombinant Alpha Synuclein S87N Mutant Monomers
• Product Name Alternative: Alpha Synuclein S87N, Alpha synuclein protein, Alpha-synuclein protein, Non-A beta component of AD amyloid protein, Non-A4 component of amyloid precursor protein, NACP protein, SNCA protein, NACP protein, PARK1 protein, SYN protein, Parkinson's disease familial 1 Protein
• UNSPSC: 12352202
• Gene ID: 6622
• Swiss Prot: P37840-1
• Accession Number: NP_000336.1
• Host: E. coli
• Origin Species: Human
• Target: Alpha Synuclein S87N Mutant
• Conjugation: No Tag
• Sequence: MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
• Applications: WB, SDS PAGE, In vitro Assay
• Purification Method: Ion-exchange Purified
• Concentration: 2 mg/ml or 5 mg/ml
• Purity: >95%
• Weight: 0.01
• Length: 140 AA
• Buffer: 1X PBS pH 7.4
• Molecular Weight: 14.46 kDa
• Precautions: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
• Additionnal Information: For corresponding PFFs, see catalog# SPR-500
• References & Citations: 1. Masuda-Suzukake et al. 2013. Prion-like Spreading of Pathological α-synuclein in Brain. Brain. https://doi.org/10.1093/braiwt037 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