Recombinant human alpha-Synuclein (1-60aa) protein

A deletion mutant of alpha-synuclein (amino acids 1-60), which contains the N-terminal amphipathic domain. alpha-Syn 1-60 was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.

Product Specifications

Product Name Alternative

SNCA, NACP, PARK1, PARK4, PD1, α-synuclein Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Parkinson disease 4, autosomal dominant Lewy body

Expression System

E.coli

Antigen Species

Human

Tag

Non-Tagged

Applications

SDS-PAGE

Concentration

1 mg/mL (determined by BCA assay)

Purity

> 95% by SDS-PAGE

Molecular Weight

6.1 kDa (60aa) confirmed by MALDI-TOF

Additionnal Information

A-Synuclein (160aa), 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, SNA3009-10 µg, SNA3009-20 µg, SNA3009-50 µg, SNA3009-100 µg, SNA3009-250 µg, SNA3009-500 µg, SNA3009-1 mg, SNA3009-10, SNA3009-20, SNA3009-50, SNA3009-100, SNA3009-250, SNA3009-500, SNA3009-1

References & Citations

Ueda., et al. (1993) Proc. Natl. Acad. Sci. 90 (23) :11282-6.; ; Jakes., et al. (1994) FEBS Letters 345, 27-32.;

Other References

Kim EJ, et al. Dyrk1A phosphorylates alpha-synuclein and enhances intracellular inclusion formation. (J Biol Chem. 2006) {https://pubmed.ncbi.nlm.nih.gov/16959772/}; ; Park JY, et al. Microglial phagocytosis is enhanced by monomeric alpha-synuclein, not aggregated alpha-synuclein: implications for Parkinsons disease. (Glia. 2008) {https://pubmed.ncbi.nlm.nih.gov/18449945/}; ; Fantini J, et al. The fusogenic tilted peptide (67-78) of α-synuclein is a cholesterol binding domain. (Biochim Biophys Acta. 2011) {https://pubmed.ncbi.nlm.nih.gov/21756873/}; ; Kawakami F, et al. Stimulatory effect of α-synuclein on the tau-phosphorylation by GSK-3β. (FEBS J. 2011) {https://pubmed.ncbi.nlm.nih.gov/21985244/}