|Product Name||HSP60 ELISA Kit|
Colorimetric detection of HSP60
|Sample Types||Cell lysates, Serum, Tissue|
|Detection Method||Colorimetric Assay|
|Assay Type||Sandwich ELISA (Enzyme-linked Immunosorbent Assay)|
|Utility||ELISA kit used to quantitate HSP60 concentration in samples.|
|Assay Range||11 - 700 ng/ml|
|Incubation Time||30 minutes|
|Number of Samples||40 samples in duplicate|
|Other Resources||, Kit Booklet Lot No. BH585599 , Kit Booklet Lot No. TH585578 , Kit Booklet Lot No. 160427 , MSDS|
|Shipping Temperature||Blue Ice|
|Product Type||ELISA Kits|
|Assay Overview||1. Prepare Standard and samples in Standard and Sample Diluent.
2. Add 100 µL of Standard or sample to appropriate wells.
3. Cover plate with Plate Sealer and incubate at 37°C for 1 hour.
4. Wash plate four times with 1X Wash Buffer.
5. Add 100 µL of Biotinylated Antibody Working Solution to each well.
6. Cover plate with Plate Sealer and incubate at 37°C for 1 hour.
7. Wash plate four times with 1X Wash Buffer.
8. Add 100 µL of Streptavidin-HRP Working Solution to each well.
9. Cover plate with Plate Sealer and incubate at room temperature for 30 minutes.
10. Wash plate four times with 1X Wash Buffer.
11. Add 100 µL of TMB Substrate to each well.
12. Develop the plate in the dark at room temperature for 30 minutes.
13. Stop reaction by adding 100 µL of Stop Solution to each well.
14. Measure absorbance on a plate reader at 450 nm.
|Cite This Product||HSP60 ELISA Kit (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SKT-110)|
|Alternative Names||CPN60 ELISA Kit, GROEL ELISA Kit, HLD4 ELISA Kit, HSP 60 ELISA Kit, HSP65 ELISA Kit, HSPD1 ELISA Kit, HuCHA60 ELISA Kit, SPG 13 ELISA Kit|
|Research Areas||Cancer, Heat Shock|
|Scientific Background||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||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.
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