HSPA1L Protein, Human (His, Strep)

HSP70 is a molecular chaperone involved in a wide range of cellular processes, including protecting the proteome from stress, folding and transporting newly synthesized polypeptides, activating proteolysis of misfolded proteins, and facilitating the formation and dissociation of protein complexes. It plays a central role in the protein quality control system by ensuring proper protein folding, refolding misfolded proteins, and regulating the targeting of proteins for degradation. This function is mediated through cycles of ATP binding, hydrolysis, and ADP release, coordinated by co-chaperones. The affinity of HSP70 for polypeptides is regulated by its nucleotide-bound state: it exhibits low substrate affinity in the ATP-bound form, but undergoes a conformational shift upon ATP hydrolysis to ADP, increasing substrate binding. Repeated cycles of ATP hydrolysis and nucleotide exchange enable substrate binding and release. Additionally, HSP70 positively regulates PRKN translocation to damaged mitochondria.