Mouse Recombinant Monoclonal Hsp60 antibody. Suitable for IHC-P and reacts with Human samples. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human HSPD1.
IgG1
Mouse
pH: 7.2 - 7.4
Preservative: 0.05% Sodium azide
Constituents: PBS
Liquid
Monoclonal
IHC-P | |
---|---|
Human | Tested |
Mouse | Predicted |
Rat | Predicted |
Chicken | Predicted |
Cow | Predicted |
Dog | Predicted |
Drosophila melanogaster | Predicted |
Hamster | Predicted |
Monkey | Predicted |
Pig | Predicted |
Rabbit | Predicted |
Sheep | Predicted |
Xenopus laevis | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 0.5-1 µg/mL | Notes (Primary incubation for 10 minutes at room temperature). Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Rat, Sheep, Rabbit, Chicken, Hamster, Cow, Dog, Pig, Xenopus laevis, Drosophila melanogaster, Monkey, Mouse | Dilution info - | Notes - |
Select an associated product type
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:11422376, PubMed:1346131). 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).
HSP60, HSPD1, HSP60, 60 kDa chaperonin, Chaperonin 60, Heat shock protein 60, Heat shock protein family D member 1, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, CPN60, HSP-60, Hsp60
Mouse Recombinant Monoclonal Hsp60 antibody. Suitable for IHC-P and reacts with Human samples. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human HSPD1.
IgG1
Mouse
pH: 7.2 - 7.4
Preservative: 0.05% Sodium azide
Constituents: PBS
Liquid
Monoclonal
rGROEL/780
Affinity purification Protein A/G
kappa
Purified from Bioreactor Concentrate by Protein A/G.
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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.
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.
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.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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Formalin-fixed, paraffin-embedded human liver tissue stained for Hsp60 using ab234295 at 1 μg/ml in immunohistochemical analysis.
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