Recombinant human alpha-Synuclein protein
Alpha-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. alpha-synuclein has been suggested to be implicated in the pathogenesis of Parkinson's disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that alpha-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140) .
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)
Endotoxin
< 1 EU per 1ug of protein (determined by LAL method)
Purity
> 95% by SDS-PAGE
Molecular Weight
14.4 kDa (140aa) confirmed by MALDI-TOF (Molecular weight on SDS-PAGE will appear higher)
Additionnal Information
A-Synuclein, 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, SNA2001-10 µg, SNA2001-20 µg, SNA2001-50 µg, SNA2001-100 µg, SNA2001-250 µg, SNA2001-500 µg, SNA2001-1 mg, SNA2001-10, SNA2001-20, SNA2001-50, SNA2001-100, SNA2001-250, SNA2001-500, SNA2001-1
References & Citations
Jakes, R., et al. (1994) FEBS lett. 345, 27-32; ; ueda, K., et al. (1993) Proc. Natl. Acad. Sci. uSA 90, 11282-11286; ; Kim, J. (1997) Molecules and Cells 7, 78-83; ; Paik, S. R., et al. (1997) Arch. Biochem. Biophys. 344, 325-334.;
Other References
Sung JY, et al. Proteolytic cleavage of extracellular secreted alpha-synuclein via matrix metalloproteinases. (J Biol Chem. 2005) {https://pubmed.ncbi.nlm.nih.gov/15863497/}; ; Ahn KJ, et al. Amino acid sequence motifs and mechanistic features of the membrane translocation of alpha-synuclein. (J Neurochem. 2006) {https://pubmed.ncbi.nlm.nih.gov/16524375/}; ; Kim EJ, et al. Dyrk1A phosphorylates alpha-synuclein and enhances intracellular inclusion formation. (J Biol Chem. 2006) {https://pubmed.ncbi.nlm.nih.gov/16959772/}; ; Lee HJ, et al. Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. (Int J Biochem Cell Biol. 2008) {https://pubmed.ncbi.nlm.nih.gov/18291704/}; ; Lee HJ, et al. Clearance and deposition of extracellular alpha-synuclein aggregates in microglia. (Biochem Biophys Res Commun. 2008) {https://pubmed.ncbi.nlm.nih.gov/18492487/}; ; 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/}; ; Lee HJ, et al. Direct transfer of alpha-synuclein from neuron to astroglia causes inflammatory responses in synucleinopathies. (J Biol Chem. 2010) {https://pubmed.ncbi.nlm.nih.gov/20071342/}; ; Kim KS, et al. Regulation of Weibel-Palade body exocytosis by alpha-synuclein in endothelial cells. (J Biol Chem. 2010) {https://pubmed.ncbi.nlm.nih.gov/20448034/}; ; Lee HJ, et al. Enzyme-linked immunosorbent assays for α-synuclein with species and multimeric state specificities. (J Neurosci Methods. 2011) {https://pubmed.ncbi.nlm.nih.gov/21658411/}; ; 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/}; ; Kim KS, et al. Proteolytic cleavage of extracellular α-synuclein by plasmin: implications for Parkinson disease. (J Biol Chem. 2012) {https://pubmed.ncbi.nlm.nih.gov/22619171/}; ; Rodriguez-Araujo G, et al. Alpha-synuclein elicits glucose uptake and utilization in adipocytes through the Gab1/PI3K/Akt transduction pathway. (Cell Mol Life Sci. 2013) {https://pubmed.ncbi.nlm.nih.gov/23124190/}; ; Kim JY, et al. Nanomolar concentration of alpha-synuclein enhances dopaminergic neuronal survival via Akt pathway. (Neural Regen Res. 2013) {https://pubmed.ncbi.nlm.nih.gov/25206648/}; ; Kim HL, et al. The Presence of Outer Arm Fucose Residues on the N-Glycans of Tissue Inhibitor of Metalloproteinases-1 Reduces Its Activity. (J Proteome Res. 2014) {https://pubmed.ncbi.nlm.nih.gov/23815085/}; ; Rodriguez-Araujo G, et al. Low alpha-synuclein levels in the blood are associated with insulin resistance. (Sci Rep. 2015) {https://pubmed.ncbi.nlm.nih.gov/26159928/}; ; Takami Y, et al. Novel pathophysiological roles of α-synuclein in age-related vascular endothelial dysfunction. (FASEB J. 2022) {https://pubmed.ncbi.nlm.nih.gov/26159928/}
Storage Conditions
Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
Formulation
Liquid in. 20 mM Tris-HCl buffer (pH 7.5) containing 0.1 M NaCl, 1mM MgCl2
Scientific Category
Neuroscience
NCBI Accession Number
NP_000336.1
Uniprot Accession Number
P37840
Species
Human
AA Sequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
Curated Selection
Explore Other Products
Discover premium biology products from our extensive collection of 20M+ items
ARP60678_P050-Biotin 100 µL
ATAD1 Antibody - N-terminal region : Biotin (ARP60678_P050-Biotin)
Ask
View Details