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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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HSP60 Antibody / Heat Shock Protein 60 Antibody detects HSP60, a highly conserved molecular chaperone encoded by the HSPD1 gene. HSP60 is primarily localized to the mitochondrial matrix, where it helps maintain protein homeostasis by assisting the folding and assembly of proteins imported into mitochondria. It belongs to the chaperonin family and functions together with the co-chaperonin HSP10 to provide a protected environment in which newly imported or stress-damaged proteins can achieve their proper conformation.
HSP60 is synthesized as a precursor containing an N-terminal mitochondrial targeting sequence that directs transport into the organelle. Following mitochondrial import, the targeting sequence is removed to generate the mature protein. HSP60 subunits assemble into oligomeric chaperonin complexes that undergo ATP-dependent conformational changes during cycles of protein folding. This activity is particularly important because most mitochondrial proteins are encoded by nuclear genes, synthesized in the cytosol, and subsequently imported into mitochondria.
Although HSP60 is best characterized as a mitochondrial chaperonin, its biological significance extends beyond constitutive protein folding. Changes in HSPD1 expression, localization, and function have been investigated in cellular stress, oxidative stress, mitochondrial dysfunction, inflammation, immunity, neurodegeneration, and cancer. HSP60 can therefore serve as an important subject for studies of mitochondrial biology, proteostasis, stress responses, and disease-associated changes in cellular homeostasis.
Mammalian HSP60 is evolutionarily related to bacterial GroEL, and the substantial conservation among chaperonins has generated interest in their roles in immune recognition and host-pathogen biology. Antibody cross-reactivity with bacterial chaperonins can vary, making the distinction between mammalian HSP60 recognition and bacterial GroEL recognition relevant when selecting reagents for these studies.
This Protein Microarray Validated HSP60 Antibody has been evaluated using the HuProt array containing more than 19,000 full-length human proteins. In protein microarray analysis, the Z-score represents signal intensity in standard deviations above the mean array signal, while the S-score measures the difference between the target Z-score and the next highest signal, providing an indication of relative target specificity.
NSJ Bioreagents offers clone rGROEL/780 as a recombinant monoclonal reagent for investigating mitochondrial chaperone biology. An HSP60 Antibody can support research into mitochondrial protein folding, proteostasis, cellular stress, and the biological functions of Heat Shock Protein 60.
Explore our Mitochondria Marker Antibody page for additional reagents targeting proteins involved in mitochondrial structure, function, metabolism, and protein homeostasis.
Optimal dilution of the HSP60 Antibody / Heat Shock Protein 60 Antibody should be determined by the researcher.
1. The prediluted format is supplied in a dropper bottle and is optimized for use in IHC. After epitope retrieval step (if required), drip mAb solution onto the tissue section and incubate at RT for 30 min.
Recombinant human protein was used as the immunogen for the recombinant HSP60 Antibody. The Its epitope has been localized between amino acids 383-447.
Store the HSP60 Antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
HSPD1 antibody, HSP60 antibody, Heat shock protein 60 antibody, 60 kDa heat shock protein mitochondrial antibody, Chaperonin 60 antibody, CPN60 antibody, HSP65 antibody, GROEL antibody
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