||Recombinant Human HSPA1A (Accession # AAD21816) was produced in E. coli-derived.
||X mg/ml (X µM) in 50 mM HEPES pH 8, 100 mM NaCl, 5 mM DTT
||HSP70/HSPA1A is a molecular chaperone that assists in the folding of nascent polypeptides and the refolding of denatured proteins, but can also promote their degradation in conjunction with specific E3 ligases, such as CHIP, if either of these processes proceeds inefficiently. Reaction conditions will need to be optimized for each specific application. We recommend an initial HSP70/HSPA1A concentration of 2-3 µM for in vitro use. IMPORTANT: HSP40/DNAJB1, or another suitable co-chaperone, is required for HSP70/HSPA1A activity and should be used at a concentration that is equimolar to HSP70/HSPA1A.
||Recombinant Human HSPA1A has a calculated MW of 70 kDa.
||>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
||Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at: In lyophilized state for 1 year (4ºC); After reconstitution under sterile conditions for 3 months (-70ºC).