Recombinant human alpha-Synuclein (61-140aa) protein

A deletion mutant of alpha-synuclein (amino acids 61-140) . Syn61-140 was overexpressed in E. coli and was purified to apparent homogeneity by taking advantage of the thermosolubility of protein and by using conventional column chromatography techniques. Additional amino acid (Met) is attached at the N-terminus.

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

8.4 kDa (81aa) confirmed by MALDI-TOF (Molecular weight on SDS-PAGE will appear higher)

Additionnal Information

A-Synuclein (61140aa), 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, SNA2006-10 µg, SNA2006-20 µg, SNA2006-50 µg, SNA2006-100 µg, SNA2006-250 µg, SNA2006-500 µg, SNA2006-1 mg, SNA2006-10, SNA2006-20, SNA2006-50, SNA2006-100, SNA2006-250, SNA2006-500, SNA2006-1

References & Citations

Park SM., et al. (2002) Blood. 100 (7) :2506-14.; ; Park SM., et al. (2002) Biochemistry. 41 (12) :4137-46.;

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/}