heat shock protein 70

Heat shock protein 70 (Hsp70) is a highly conserved family of molecular chaperone proteins found in virtually all living organisms. It plays a crucial role in cellular protection against various forms of physiological stress by assisting in the proper folding of nascent and stress-accumulated misfolded proteins, preventing aggregation, and facilitating the refolding or degradation of damaged proteins. Hsp70 also inhibits both caspase-dependent and caspase-independent apoptosis, thereby promoting cell survival under adverse conditions[1][2][3]. In addition to its intracellular functions, membrane-bound and extracellular forms have been identified with potential roles as therapeutic targets in cancer and neurodegenerative diseases[2]. Recombinant or exogenous Hsp70 has demonstrated tissue-protective effects in models of ischemic injury, neurodegeneration, inflammation, and cardiovascular disease[6]. Pharmacological induction or administration of recombinant Hsp70 is being explored for its neuroprotective properties as well as immunomodulatory effects relevant to oncology (e.g., cancer vaccines)[3][5][7].

Other names

70 kilodalton heat shock proteinHSP70HSP-70HSP 70recombinant 70-kD heat-shock proteinrecombinant70-kD heat-shock proteinrecombinant-70-kD heat-shock protein