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Hsp60 StressXpress® Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:CPN60, GROEL, HLD4, Hsp 60, Hsp65, HSPD1, HuCHA60, SPG 13
  • Species:Human
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Cat. No. Size Price


RSKT-110-480R 5x 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Tissue extract, Cell lysate

Storage/Expiration

2–8°C

Calibration Curve

Calibration Range

7–450 ng/mL

Limit of Detection

1.37 ng/mL

Summary

Features

  • ELISA kit used to quantitate Hsp60 concentration in samples
  • The total assay time is less than 4 hours

Research topic

Apoptosis, Immune Response, Infection and Inflammation, Others

Summary

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 heat shock proteins 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 (1-3). 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 environmental stress such as 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 groE operon is under strict regulatory control. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of Hsp60 and Hsp10 is their protective functions against infection and cellular stress. Hsp60 has however been linked to a number of autoimmune diseases, as well as Alzheimers, coronary artery diseases, MS, and diabetes (6-9

References to Summary

References to Heat Shock 60kDa Protein

  • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell. 1998 Feb 6;92 (3):351-66
  • Deocaris CC, Kaul SC, Wadhwa R. On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60. Cell Stress Chaperones. 2006 Summer;11 (2):116-28
  • Gupta S, Knowlton AA. HSP60, Bax, apoptosis and the heart. J Cell Mol Med. 2005 Jan-Mar;9 (1):51-8
  • Hartl FU. Molecular chaperones in cellular protein folding. Nature. 1996 Jun 13;381 (6583):571-9
  • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 2002 Mar 8;295 (5561):1852-8
  • Itoh H, Komatsuda A, Ohtani H, Wakui H, Imai H, Sawada K, Otaka M, Ogura M, Suzuki A, Hamada F. Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration. Eur J Biochem. 2002 Dec;269 (23):5931-8
  • Jindal S, Dudani AK, Singh B, Harley CB, Gupta RS. Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen. Mol Cell Biol. 1989 May;9 (5):2279-83
  • Lai HC, Liu TJ, Ting CT, Yang JY, Huang L, Wallace D, Kaiser P, Wang PH. Regulation of IGF-I receptor signaling in diabetic cardiac muscle: dysregulation of cytosolic and mitochondria HSP60. Am J Physiol Endocrinol Metab. 2007 Jan;292 (1):E292-7
  • LaVerda D, Kalayoglu MV, Byrne GI. Chlamydial heat shock proteins and disease pathology: new paradigms for old problems?. Infect Dis Obstet Gynecol. 1999;7 (1-2):64-71
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