SNCA 1-95, Human
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
Greater than 95.0% as determined by SDS-PAGE.
Description
SNCA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (1-95 a.a.) and having a molecular mass of 9.3kDa.
SNCA is purified by proprietary chromatographic techniques.
Product Specs
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFV
Product Science Overview
Alpha-Synuclein 1-95 is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain with a molecular mass of approximately 9.3 kDa . The recombinant protein is typically purified using proprietary chromatographic techniques to ensure high purity and low endotoxin levels .
Alpha-synuclein functions as a monomer in synaptic vesicle exocytosis, enhancing vesicle priming, fusion, and dilation of exocytotic fusion pores . It increases local calcium release from microdomains, which is essential for the enhancement of ATP-induced exocytosis . Additionally, in its multimeric membrane-bound state, alpha-synuclein acts as a molecular chaperone, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at the presynaptic plasma membrane .
Alpha-synuclein is extensively studied in the context of neurodegenerative diseases, particularly Parkinson’s disease. The protein is a major component of Lewy bodies, which are pathological hallmarks of Parkinson’s disease and other synucleinopathies. Phosphorylation of alpha-synuclein, especially at serine-129, is a common post-translational modification observed in these diseases and is associated with the formation of insoluble fibrils .
Recombinant human alpha-synuclein 1-95 is widely used in research to study the protein’s structure, function, and role in disease. It is suitable for various applications, including SDS-PAGE, Western blotting (WB), and other biochemical assays . The availability of high-purity recombinant protein allows researchers to investigate the molecular mechanisms underlying alpha-synuclein’s involvement in synaptic activity and neurodegeneration.
