| Field | Specification |
|---|---|
| Accession Number | |
| Alternative Names | HSPD1, HSP60, 60 kDa heat shock protein, mitochondrial, Chaperonin 60, CPN60, HuCHA60, Heat shock protein family D member 1, GroEL homolog, mitochondrial, GROEL, HLD4, HSP 60, HSP65, SPG 13 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | Human HSP60 produced through recombinant DNA methods in E.coli |
| Product Type | |
| Reactivity | |
| Shipping | |
| Storage | |
| Target |
HSP60, also known as Cpn60 or GroEL in prokaryotes, is a highly conserved molecular chaperone essential for protein folding and cellular homeostasis. Present in both prokaryotic and eukaryotic cells, HSP60 prevents protein misfolding and aggregation during biogenesis and under stress conditions. In mammals, HSP60 is localized to the mitochondria, where it partners with its co-chaperonin HSP10 to facilitate the proper folding and assembly of mitochondrial proteins.
Structurally, HSP60 forms homo-oligomeric complexes of 7 or 14 subunits, exhibiting ATPase activity and reversible dissociation in the presence of Mg²⁺ and ATP. Its evolutionary conservation is underscored by the ability of human HSP60-HSP10 to functionally replace the bacterial GroEL-GroES system in engineered E. coli strains.
Beyond its canonical role in mitochondrial proteostasis, HSP60 has been implicated in immune regulation and cellular stress responses. Elevated levels of HSP60 have been associated with several chronic diseases, including autoimmune disorders, coronary artery disease, diabetes, and neurodegenerative conditions such as Alzheimer’s disease and multiple sclerosis.
In neuroscience, HSP60’s role in maintaining mitochondrial integrity is particularly significant, as mitochondrial dysfunction is a central feature of many neurodegenerative diseases. Its dual function in protein quality control and cellular protection positions HSP60 as a promising biomarker and therapeutic target in neurodegeneration research.
1 µg/ml of SPC-105 was sufficient for detection of HSP60 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using goat anti-mouse IgG as the secondary antibody.
Cite this product varies by variant:
- SPC-105D — Size: 100 ug: HSP60 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D, RRID: AB_10807230)
- SPC-105D-A390 — Size: 100 ug: HSP60 Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-A390, RRID: AB_2703211)
- SPC-105D-A488 — Size: 100 ug: HSP60 Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-A488, RRID: AB_2703212)
- SPC-105D-A594 — Size: 100 ug: HSP60 Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-A594, RRID: AB_2703214)
- SPC-105D-APC — Size: 100 ug: HSP60 Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-APC, RRID: AB_2703220)
- SPC-105D-BI — Size: 100 ug: HSP60 Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-BI, RRID: AB_2703221)
- SPC-105D-FITC — Size: 100 ug: HSP60 Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-FITC, RRID: AB_2703222)
- SPC-105D-HRP — Size: 100 ug: HSP60 Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-HRP, RRID: AB_2703223)
- SPC-105D-PCP — Size: 100 ug: HSP60 Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-PCP, RRID: AB_2703225)
- SPC-105D-RPE — Size: 100 ug: HSP60 Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105D-RPE, RRID: AB_2703226)
- SPC-105S — Size: 12 ug: HSP60 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SPC-105S, RRID: AB_10807230)
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
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.
10. Gao, Y.L., et al (1995) J. of Immunology 154: 3548-3556.
11. Neuer, A., et al (1997) European Society for Human Reproduction and Embryology 12(5):925-929.
12. Bason, C., et al (2003) Lancet 362(9400): 1971-1977.
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