HSP70/HSPA1A, Human (E110D, His)

The HSP70/HSPA1A protein is an important molecular chaperone that protects proteome integrity by counteracting stress, aiding protein folding, activating misfolded proteolysis, and regulating protein complex dynamics. In protein quality control systems, it ensures accurate protein folding, controls substrate targeting for degradation through the ATP cycle, and interacts with co-chaperones such as HSP40, BAG1/2/3, HOPX, and STUB1. HSP70/HSPA1A Protein, Human (E110D, His) is the recombinant human-derived HSP70/HSPA1A protein, expressed by E. coli , with N-His labeled tag and E110D, , , , mutation. The total length of HSP70/HSPA1A Protein, Human (E110D, His) is 640 a.a., with molecular weight of 72.2 kDa.