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Target: Alpha Synuclein S87N Mutant
Nature: Recombinant
Swiss-Prot: P37840-1
Expression System: E. coli
Protein Length: 140 AA
Amino Acid Sequence: MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
Purification: Ion-exchange Purified
Purity: >95%
Storage Buffer: 1X PBS pH 7.4
Protein Size: 14.46 kDa
Conjugate: No Tag
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.
References: 1. Masuda-Suzukake et al. 2013. Prion-like Spreading of Pathological α-synuclein in Brain. Brain. https://doi.org/10.1093/brain/awt0372. 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/ja203979j3. Ohgita, T. et al. 2023. Intramolecular Interaction Kinetically Regulates Fibril Formation by Human and Mouse Alpha-Synuclein. Sci Rep https://doi.org/10.1038/s41598-023-38070-44. 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
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
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