Heat shock protein (HSP) is a protein induced by various stressors such as damage, cold, UV exposure, and tissue repair in the body. It is related to improving the tolerance and stress ability of cells to damage and exists in most organisms, mainly induced by a certain degree of stimulation. HSP70 is the most abundant heat stress protein in the HSP family of proteins, widely present in animals, plants, and microorganisms, and plays the role of a "guardian". Its main functions are manifested in tolerance to cellular immunity, innate immune response, antioxidant, anti apoptotic, and molecular pairing. At the same time, HSP70 also participates in and regulates protein folding modification. The widespread and multifunctional distribution of HSP70 makes it one of the most studied stress proteins. HSP70 has a molecular weight of approximately 70kD and is known as the main heat shock protein, including over 20 proteins with molecular weights of 68, 72, 73, 75, 78kDa, etc. The HSP70 family proteins have similar molecular weights, isoelectric points between pH 5.2 and 6.3, and similar trypsin peptide profiles. They are often highly induced in stress cells of almost all organisms and have protective functions for the body and cells. Under normal circumstances, HSP70 is located in the cytoplasm. When stimulated by heat shock, HSP70 rapidly increases in the nucleus, with only a small amount present in the cytoplasm. When the cell is in the recovery stage, HSP70 disappears in the nucleus, and low levels of HSP70 expression are still present in the cytoplasm.