HEAt shock protein 60 (Hsp60), also known as hEAt shock protein family D member 1 (HspD1), is an approximately 60 kDa protein that functions as a molecular chaperone.1 It belongs to the type I subclass of chaperonins and is found in eubacteria, mitochondria, and chloroplasts where its expression is induced by stress. Hsp60 primarily exists as a heptameric ring that it is converted to a tetradecameric double-ring structure in the presence of ATP.2 Within mitochondria, it associates with its co-chaperone, Hsp10, to form a barrel-like structure and refold proteins that have been shuttled to the mitochondria in an ATP-dependent manner.2,3 Hsp60 also has extramitochondrial functions such as the production of proinflammatory cytokines in human leukocytes and activation of innate immune receptors.4,5 Hsp60 expression is incrEAsed in the serum and saliva of patients with type 2 diabetes mellitus and mutations in HSPD1 lEAd to neurodegenerative disEAses.5,6Technical InformationSynonymsChaperonin 60Cpn60HEAt Shock Protein 60HSPD1Mitochondrial Matrix Protein P1Purity90% estimated by SDS-PAGESourceActive N-terminal Histidine-tagged human Hsp60 protein (full length) purified from E. coliAmino Acids2-573 (full length)MW63.27 kDaStorage Buffer50 mM HEPES, pH 8.0, 150 mM sodium chloride