Recombinant Human His6-alpha-Synuclein Protein, CF
Recombinant Human His6-alpha-Synuclein Protein, CF Summary
Recombinant Human His6-alpha -Synuclein is ideal for use as a control substrate for in vitro Ubiquitin conjugation using select Ubiquitin E3 ligases such as CHIP/Stub1. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human His6-alpha -Synuclein concentration of 0.5-2.5 μM.
Contains a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Supplied as a solution in HEPES and NaCl.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
alpha -Synuclein is member of a family of small soluble proteins that include also beta -, and gamma -Synuclein. It is predominantly expressed in neurons of the central nervous system in the presynaptic region of nerve terminals, where cycles between free partially unfolded and helical membrane-bound forms. alpha -Synuclein can self-aggregate in vivo and in vitro, forming various oligomeric species and fibrillar and amorphous aggregates. The fibrils and amyloidal forms of alpha -Synuclein are major components of Lewy bodies and Lewy neurites and have been linked to the pathogenesis of Parkinson’s disease, Parkinson’s disease dementia, and dementia with Lewy bodies. alpha -Synuclein aggregates can be also found associated with amyloid plaques in Alzheirmer’s disease.
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