Antigen: human recombinant Hsp60 · Clone designation: LK-1 · Host: mouse · Isotype: IgG₁ · Application(s): WB, IP, flow cytometry, and EIA · In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the Hsp60 family of Hsps are some of the best characterized chaperones. Hsp60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian Hsp60.^1,2,3 Whereas mammalian Hsp60 is localized within the mitochondria, plant Hsp60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that Hsp60 is present in so many different species. The common characteristics of the Hsp60s from the divergent species are i) high abundance; ii) induction with enviromental stress such as a heat shock; iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP; iv) ATPase activity; and v) a role in folding and assembly of oligomeric protein structures.⁴ These similarities are supported by recent studies where the single-ring human mitochondrial homolog, Hsp60 with its co-chaperonin, Hsp10 were expressed in a E. coli strain, engineered so that the Hsp60 operon is under strict regulatory control.

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Hartl, F.U. Molecular chaperones in cellular protein folding. Nature 381 571-580 (1996).

Hartl, F.U., and Hayer-Hartl, M. Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295(5561) 1852-1858 (2002).

Jindal, S., Dudani, A.K., Singh, B., et al. Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperones and to the 65-kilodalton mycobacterial antigen. Mol Cell Biol 9(5) 2279-2283 (1989).

Lai, H., Liu, T., Ting, C., et al. Regulation of IGF-I receptor signaling in diabetic cardiac muscle: Dysregulation of cytosolic and mitochondria Hsp60. Am J Physiol Endocrinol Metab 292 E292-E297 (2007).

Deocaris, C.C., Kaul, S.C., and Wadhwa, R. On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60. Cell Stress Chaperones 11(2) 116-128 (2006).

Gupta, S., and Knowlton, A.A. Hsp60, bax, apoptosis and the heart. J Cell Mol Med 9(1) 51-58 (2005).

Itoh, H., Komatsuda, A., Ohtani, H., et al. Mammalian Hsp60 is quickly sorted into the mitochondria under conditions of dehydration. Eur J Biochem 269 5931-5938 (2002).

LaVerda, D., Kalayoglu, M.V., and Byrne, G.I. Chlamydial heat shock proteins and disease pathology: New paradigms for old problems? Infect Dis Obstet Gynecol 7 64-71 (1999).

Bukau, B., and Hornwich, A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92 351-366 (1998).

Bason, C., Corrocher, R., Lunardi, C., et al. Interaction of antibodies against cytomegalovirus with heat-shock protein 60 in pathogenesis of atherosclerosis. Lancet 362 1971-1977 (2003).

Neuer, A., Lam, K., Tiller, F., et al. Humoral immune response to membrane components of Chlamydia trachomatis and expression of human 60 kDa heat shock protein in follicular fluid of in vitro fertilization patients. Hum Reprod 12(5) 925-929 (1997).

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