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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.

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Images

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp60 antibody [rGROEL/780] - BSA free (AB234295), expandable thumbnail

Key facts

Isotype

IgG1

Host species

Mouse

Storage buffer

pH: 7.2 - 7.4
Preservative: 0.05% Sodium azide
Constituents: PBS

Form

Liquid

Clonality

Monoclonal

Immunogen

  • Recombinant Full Length Protein corresponding to Human HSPD1. Database link P10809

Reactivity data

Select an application
Product promiseTestedExpectedPredictedNot recommended
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

Tested
Tested

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.

Predicted
Predicted

Species

Rat, Sheep, Rabbit, Chicken, Hamster, Cow, Dog, Pig, Xenopus laevis, Drosophila melanogaster, Monkey, Mouse

Dilution info

-

Notes

-

Associated Products

Select an associated product type

7 products for Alternative Product

Target data

Function

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).

Alternative names

Recommended products

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.

Key facts

Isotype

IgG1

Form

Liquid

Clonality

Monoclonal

Immunogen
  • Recombinant Full Length Protein corresponding to Human HSPD1. Database link P10809
Clone number

rGROEL/780

Purification technique

Affinity purification Protein A/G

Light chain type

kappa

Concentration
Loading...
Purification notes

Purified from Bioreactor Concentrate by Protein A/G.

Storage

Shipped at conditions

Blue Ice

Appropriate short-term storage duration

1-2 weeks

Appropriate short-term storage conditions

+4°C

Appropriate long-term storage conditions

-20°C

Aliquoting information

Upon delivery aliquot

Storage information

Avoid freeze / thaw cycle

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

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.

Associated diseases and disorders

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.

Product promise

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1 product image

  • Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp60 antibody [rGROEL/780] - BSA free (ab234295), expandable thumbnail

    Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Hsp60 antibody [rGROEL/780] - BSA free (ab234295)

    Formalin-fixed, paraffin-embedded human liver tissue stained for Hsp60 using ab234295 at 1 μg/ml in immunohistochemical analysis.

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can:

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