protein

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

SNA3009

20 ug

55 USD

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

1-60aa

SNA3009

NP_000336.1

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.

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

1mg/ml (determined by BCA assay)

Liquid in. 20mM Tris-HCl buffer (pH 7.5) containing 0.1M NaCl

Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

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

> 95% by SDS-PAGE

SDS-PAGE

Human

Neuroscience

6.1 kDa (60aa) confirmed by MALDI-TOF

MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK

Non-Tagged

E.coli

Recombinant Protein

P37840

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,SNA3009-10ug,SNA3009-20ug,SNA3009-50ug,SNA3009-100ug,SNA3009-250ug,SNA3009-500ug,SNA3009-1mg,SNA3009-10,SNA3009-20,SNA3009-50,SNA3009-100,SNA3009-250,SNA3009-500,SNA3009-1

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/}