Description
Key facts
Detection method:Colorimetric,
Sample types:Serum,
Reacts with:Human,
Assay type:Indirect,
Sensitivity:= 2.88 ng/mL,
Range:7.81 - 250 ng/mL,
Assay time:1h 15m,
Assay Platform:Microplate
Product details:
Abcam's Human Anti-HSP60 IgG/A/M
in vitro
ELISA (Enzyme-Linked Immunosorbent Assay) kit is designed for the accurate quantitative measurement of Human Anti-HSP60 in Human Serum. This assay allows determination of IgG, IgA and IgM antibodies (total) to Human Hsp60 in serum.
A recombinant Human Hsp60 protein has been precoated onto 96-well plates. Standards or test samples are added to the wells, incubated and then washed. An anti-Human GAM-HRP conjugated antibody is then added and incubated. The plate is washed once more and the TMB substrate is then added which HRP catalyzes, generating a blue coloration after incubation. A stop solution is added which generates conversion to yellow color read at 450 nm which is proportional to the amount of analyte bound.
HSP60 is a member of the chaperonin family of heat shock proteins, with homologs functioning in the cytosol and mitochondria to fold nascent and aggregated proteins. HSP60 is the eukaryotic homolog of the
E. coli
GroEL protein, and forms a multimeric complex in the mitochondria with Hsp10 (Cpn10) to form a large central cavity in which ATP-dependent protein folding takes place. TRiC/CCT, a eukaryotic relative of HSP60, is expressed in the cytosol and participates in the folding of actin and tubulin substrates, but lacks any association with an Hsp10-like co-factor.
Plates are not provided
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-Multi, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Hsp60 also known as HSPD1 and heat shock protein 60 is a significant chaperonin with a molecular weight of approximately 60 kDa. It resides predominantly in the mitochondria and functions to assist in the proper folding of proteins preventing their aggregation. Hsp60 is expressed mainly in cells with high metabolic activity. Its presence as a mitochondrial marker highlights its essential role in maintaining cellular homeostasis and function.
Biological function summary
The protein ensures mitochondrial protein stability by facilitating the refolding of misfolded proteins and cooperating with other chaperonins like Hsp10. Hsp60 participates in forming a complex with these proteins to create a conducive environment for protein folding. It plays a part in regulating mitochondrial homeostasis impacting cell survival and apoptosis processes.
Pathways
Hsp60 links to the ATP synthesis and apoptosis pathways showcasing its importance as a mitochondrial marker. It interacts with proteins like caspase-3 to modulate cell death mechanisms highlighting its influence beyond simple protein folding. In the ATP synthesis pathway it contributes indirectly to energy production by maintaining mitochondrial function.
Hsp60 shows a connection to neurodegenerative diseases and cancer. Altered Hsp60 levels correlate with increased apoptosis in neurodegenerative conditions like Alzheimer's disease. Additionally in cancer interactions with proteins such as AKT suggest its potential role in cell proliferation and survival. Understanding its role could aid in the development of therapeutic interventions targeting mitochondrial dysfunction.
