|Product Name||HSP60 ELISA Kit|
|Description||Colorimetric detection of HSP60. 96wells/kit, with removable strips.|
|Cite This Product||HSP60 ELISA Kit (Boster Biological Technology, Pleasanton CA, USA, Catalog # EK7111)|
|Cross Reactivity||There is no detectable cross-reactivity.|
|Pack Size||96wells/kit, with removable strips.|
*Sensitivity, or Lower Limit of Detection (LLD), is the minimum level of target protein the ELISA assay can detect. We measure 20 blank wells and if the O.D. value is 2 standard deviations higher than the blanks' average O.D. the sample can be deemed positive.
|Assay Range||1.56 - 100 ng/ml|
*This assay range is determined using common samples. For samples with low target protein concentrations, users can adjust the standard curve to extend the lower limit of assay range.
|Sample Type||Cell lysates, Serum, Tissue|
*The above listed samples are the ones valided with the assay. If you do not see your sample of interest listed, as long as there is enough level of target protein present in the sample, this Picokine? ELISA kit should detect it.
**For protocol and tips regarding preparing your sample of interest, please check our ELISA sample preparation guide.
|Storage||Store at 4°C.|
|Anti-Hsp60 Immunoassay Plate||1 Plate|
|5X Hsp60 Extraction Reagent||1 vial/10 ml|
|Recombinant Hsp60 Standard||2 vials|
|Standard and Sample Diluent||1 vial/ 50 ml|
|10X Wash Buffer Concentrate||1 vial/100 ml|
|Anti-Hsp60 Biotinylated Antibody Concentrate||1 vial/150 μl|
|Anti-Hsp60 Biotinylated Antibody Diluent||1 vial/ 13 ml|
|Streptavidin: HRP Concentrate||1 vial/150 μl|
|Streptavidin: HRP Diluent||1 vial/ 13 ml|
|TMB Substrate||1 vial/ 13 ml|
|Stop Solution||1 vial/ 13 ml|
|Protein Name||60 kDa heat shock protein, mitochondrial|
|Protein Function||Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).|
|Subcellular Localization||Mitochondrion matrix.|
|Alternative Names||60 kDa heat shock protein, mitochondrial; 60 kDa chaperonin; Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; Hsp60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; HSPD1; HSP60|
|Research Areas||Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Organelle Markers, Protein Trafficking, Tags and Cell Markers||
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. 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. 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. 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.
Typical Standard Curve for the HSP60 ELISA Kit (Enzyme-Linked Immunosorbent Assay)–EK7111 Assay Type: Sandwich ELISA. Detection Method: Colorimetric Assay. Assay Range: 1.56 – 100 ng/ml.