| Field | Specification |
|---|---|
| Mfr No | |
| 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 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human Hsp60/HSPD1 recombinant protein (Position: A260-Q496). Human Hsp60 shares 97% amino acid (aa) sequence identity with both mouse and rat Hsp60. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-Hsp60/HSPD1 Antibody Picoband® (monoclonal, 6G2) is an antibody for HSPD1 detection raised in Mouse (Monoclonal, clone Clone: 6G2, Mouse IgG1), with reported reactivity: Human,Mouse,Rat. Commonly used in WB, IHC, IF, ICC, Flow Cytometry, ELISA workflows.
Key elements and design rationale
- Target: HSPD1 (heat shock protein family D (Hsp60) member 1); UniProt: P10809
- Antibody format: Mouse, Monoclonal, clone Clone: 6G2, Mouse IgG1
- Molecular weight: 60 kDa
- Applications: WB, IHC, IF, ICC, Flow Cytometry, ELISA
Vendor description (summary): Boster Bio Anti-Hsp60/HSPD1 Antibody Picoband® (monoclonal, 6G2) catalog # M01280-3.
Biological background
Biological context: 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. 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.
Expression and localization notes: cellular localization: Mitochondrion matrix., tissue context: Widely expressed. Overexpressed in prostate cancer..
Common research applications
- Western blotting (WB): Compare HSPD1 levels across samples and conditions using appropriate loading and biological controls.
- Immunohistochemistry (IHC): Evaluate spatial distribution of HSPD1 in tissue sections, considering fixation and antigen retrieval effects.
- Immunofluorescence / ICC: Assess subcellular localization patterns and co-localization with compartment markers in cultured cells.
- Flow cytometry: Quantify HSPD1-positive populations in single-cell suspensions with appropriate gating and controls.
- ELISA: Use antibody-based detection formats to assess antigen presence or binding in plate-based assays.
Notes for experimental interpretation
- Account for isoforms, post-translational modifications, and sample-specific processing that can shift apparent molecular weight or epitope accessibility.
- Use positive/negative biological controls where possible (e.g., known-expressing cells/tissues, knockdown/knockout models) and include appropriate secondary-only/isotype controls for imaging workflows.
Additional product notes (from provided fields)
- Specificity: No cross reactivity with other proteins.
- Background: HSP60 is a member of the chaperonin class of protein factors, which include the Escherichia coli groEL protein and the Rubisco subunit-binding protein of chloroplasts. It acts as a costimulator of human regulatory CD4-positive/CD25 -positive T cells, which inhibit lymphoproliferation and IFNG and TNF secretion by CD4-positive and CD8-positive T cells. HSP60 enhances Treg activity via TLR2, leading to activation of an intracellular signaling cascade that included p38, as well as inhibition of ERK phosphorylation. Suppression of target T cells is mediated by both cell-to-cell contact and by secretion of TGFB and IL10, and it leads to downregulation of ERK, NFKB, and TBET expression. The self-molecule HSP60 can downregulate adaptive immune responses by upregulating Tregs through TLR2 signaling.
- Cross reactivity: No cross-reactivity with other proteins.
- Cellular localization: Mitochondrion matrix.
- Tissue details: Widely expressed. Overexpressed in prostate cancer.
- Research category: Cancer,Cell Biology,Cell Cycle,Cell Cycle Inhibitors,Deubiquitination,Epigenetics and Nuclear Signaling,Host-Virus Interaction,Interspecies Interaction,Microbiology,p53 Pathway,Proteasome / Ubiquitin,Proteolysis/Ubiquitin,Ubiquitin & Ubiquitin Like Modifiers
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.
