HSP60 Antibody, Clone LK1

HSP60, also known as Cpn60 or GroEL in prokaryotes, is a highly conserved molecular chaperone essential for protein folding and cellular homeostasis. Present in both prokaryotic and eukaryotic cells, HSP60 prevents protein misfolding and aggregation during biogenesis and under stress conditions. In mammals, HSP60 is localized to the mitochondria, where it partners with its co-chaperonin HSP10 to facilitate the proper folding and assembly of mitochondrial proteins. Structurally, HSP60 forms homo-oligomeric complexes of 7 or 14 subunits, exhibiting ATPase activity and reversible dissociation in the presence of Mg²⁺ and ATP. Its evolutionary conservation is underscored by the ability of human HSP60-HSP10 to functionally replace the bacterial GroEL-GroES system in engineered E. coli strains. Beyond its canonical role in mitochondrial proteostasis, HSP60 has been implicated in immune regulation and cellular stress responses. Elevated levels of HSP60 have been associated with several chronic diseases, including autoimmune disorders, coronary artery disease, diabetes, and neurodegenerative conditions such as Alzheimer’s disease and multiple sclerosis. In neuroscience, HSP60’s role in maintaining mitochondrial integrity is particularly significant, as mitochondrial dysfunction is a central feature of many neurodegenerative diseases. Its dual function in protein quality control and cellular protection positions HSP60 as a promising biomarker and therapeutic target in neurodegeneration research.

HSPD1, HSP60, 60 kDa heat shock protein, mitochondrial, Chaperonin 60, CPN60, HuCHA60, Heat shock protein family D member 1, GroEL homolog, mitochondrial, GROEL, HLD4, HSP 60, HSP65, SPG 13

0.05 µg/ml of SMC-110 was sufficient for detection of HSP60 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using goat anti-mouse IgG as the secondary antibody.

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1. Hartl, F.U. (1996) Nature 381: 571-579. 2. Bukau, B. and Horwich, A.L. (1998) Cell 92: 351-366. 3. Hartl, F.U. and Hayer-Hartl, M. (2002) Science 295: 1852- 1858. 4. Jindal, S., et al. (1989) Molecular and Cellular Biology 9: 2279-2283. 5. La Verda, D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh, H. et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7. Gupta, S. and Knowlton, A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris, C.C. et al. (2006) Cell Stress Chaperones 11: 116-128. 9. Lai, H.C. et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297. 10. Gao, Y.L., et al (1995) J. of Immunology 154: 3548-3556. 11. Neuer, A., et al (1997) European Society for Human Reproduction and Embryology 12 (5) :925-929. 12. Bason, C., et al (2003) Lancet 362 (9400) : 1971-1977.

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