Heat shock proteins (HSPs) are a group of proteins with molecular weights less than 100 kDa, and their production increases primarily when cells are exposed to high temperatures (42-46°C). Proteins in this family are classified into six general families based on their molecular weights: HSP 100, HSP 90, HSP 70, HSP 60, small HSP proteins, and ubiquitin. Heat shock proteins play a role in many pathological conditions, such as autoimmune diseases, infectious diseases, and heart disease.

HSP 70 family comprises molecular chaperones found in many compartments of the eukaryotic cell and expressed under stress. This family of HSPs facilitates the correct folding of newly synthesized proteins, the refolding of misfolded or denatured proteins, and the degradation of damaged proteins. It also participates in proteins that facilitate translocation from membranes to organelles and influences the aggregation of misassembled proteins. I.Ş.P.70 is one of the most important cellular proteins that helps cells regain their normal structure and function. I.Ş.P.70 performs these functions through an ATP/ADP-dependent reaction cycle.