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Recombinant Human Hsp60 protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.

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SDS-PAGE - Recombinant Human Hsp60 protein (AB56277), expandable thumbnail

Key facts

Purity
>95% SDS-PAGE
Expression system
Escherichia coli
Tags
Tag free
Applications
SDS-PAGE, FuncS
Biologically active
No

Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Application
FuncS
Reactivity
Reacts
Dilution info
-
Notes

-

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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

Recombinant Human Hsp60 protein is a Human Full Length protein, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.

Key facts

Purity
>95% SDS-PAGE
Expression system
Escherichia coli
Applications
SDS-PAGE, FuncS
Accession
P10809-1
Animal free
No
Species
Human
Concentration
Loading...
Storage buffer

pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.0038% EGTA, 0.00292% EDTA, 0.00174% PMSF

Sequence info

Amino acid sequence

Accession
P10809
Protein length
Full Length
Nature
Recombinant

Specifications

Form
Liquid

General info

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).

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Subcellular localisation
Mitochondrion matrix

Storage

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°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.

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1 product image

  • SDS-PAGE - Recombinant Human Hsp60 protein (ab56277), expandable thumbnail

    SDS-PAGE - Recombinant Human Hsp60 protein (ab56277)

    SDS-PAGE analysis of ab56277 with molecular weight markers. Approximate molecular weight 85kDa.

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Product protocols

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