Description
Recombinant Mouse α-Synuclein/SNCA Protein (His Tag) | PKSM041186 | Gentaur US, UK & Europe Disrtribition
Synonyms: Alpha-synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP; Snca
Active Protein: N/A
Activity: Recombinant Mouse alpha-Synuclein is produced by our E.coli expression system and the target gene encoding Met1-Ala140 is expressed with a 6His tag at the N-terminus.
Protein Construction: Recombinant Mouse alpha-Synuclein is produced by our E.coli expression system and the target gene encoding Met1-Ala140 is expressed with a 6His tag at the N-terminus.
Fusion Tag: N-6His
Species: Mouse
Expressed Host: E.coli
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 15.9 kDa
Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Reconstitution: Please refer to the printed manual for detailed information.
Background: Alpha-synuclein (Snca) belongs to a family of proteins including a-, b-, and g-synucleins. Alpha-synuclein has been found to be implicated in the pathophysiology of many neurodegenerative diseases, including Parkinson's disease (PD) and Alzheimer's disease. Manyneurodegenerative diseases has shown that alpha-synuclein accumulates in dystrophic neurites and in Lewy bodies. The function of alpha-synuclein is closely correlated with its three-dimensional structure, especially for proteins important in the pathogenesis of neurodegenerative diseases. Alpha-synuclein is a dynamic molecule whose secondary structure depends on the environment. For example, it has an unfolded random coil structure in aqueous solution, forms a-helical structure upon binding to acidic phospholipid vesicles, and forms insoluble fibrils with a high b-sheet content that resemble the filaments found in Lewy bodies. Also, alpha-synuclein was known to associate with 14-3-3 proteins including protein kinase C, BAD, and extracellular regulated kinase, and overexpression of alpha-synuclein could contribute to cell death in neurodegenerative diseases.
Research Area: N/A
