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Overview
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HSP70 is encoded by the HSPA gene family which includes many variants of the gene. It is approximately 70kDa. There are numerous members of the HSP70 heat shock protein. HSP70 is localised to the cytoplasm. It colocalizes with SHCBP1L at spindle during the meiosis process. HSP70 is a molecular chaperone that is implicated in a wide variety of cellular processes such as the quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. It is also considered a cellular thermometer in response to heat stress and other stimuli. HSP70 is expressed in nearly every cellular compartment in eukaryotes. Mutations in the HSPA gene result in protein folding disorders, autoimmune diseases and cancer. STJ96789 was developed from clone 3G10. The antibody was affinity-purified from mouse ascites by affinity-chromatography using specific immunogen. This primary antibody binds endogenous HSP70.
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Overview