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AB78792

Recombinant Human Hsp60 protein (His tag N-Terminus)

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(3 Publications)

Recombinant Human Hsp60 protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

HSP60, HSPD1, 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

1 Images
SDS-PAGE - Recombinant Human Hsp60 protein (AB78792)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Hsp60 protein (AB78792)

SDS-PAGE analysis of ab78792 at 3μg under reducing condition.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P10809

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.3025% Tris, 0.077% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P10809","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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.
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.

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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Specifications

Form

Liquid

Additional notes

ab78792 is purified using conventional chromatography techniques.

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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

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Product protocols

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Target data

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).
See full target information HSPD1
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Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Frontiers in immunology 16:1549739 PubMed40160814

2025

The impact of the mRNA COVID-19 vaccine on the Th-like cytokine profile in individuals with no history of COVID-19: insights into autoimmunity targeting heat shock proteins.

Applications

Unspecified application

Species

Unspecified reactive species

Stefan Tukaj,Magdalena Sitna,Krzysztof Sitko

Cell stress & chaperones 26:735-740 PubMed34080135

2021

Autoantibodies to heat shock protein 60, 70, and 90 are not altered in the anti-SARS-CoV-2 IgG-seropositive humans without or with mild symptoms.

Applications

Unspecified application

Species

Unspecified reactive species

Jagoda Mantej,Marta Bednarek,Krzysztof Sitko,Marta Świętoń,Stefan Tukaj

NPJ Regenerative medicine 1: PubMed28936359

2016

Extracellular HSP60 triggers tissue regeneration and wound healing by regulating inflammation and cell proliferation.

Applications

Unspecified application

Species

Unspecified reactive species

Wuhong Pei,Katsuya Tanaka,Sunny C Huang,Lisha Xu,Baoying Liu,Jason Sinclair,Jennifer Idol,Gaurav K Varshney,Haigen Huang,Shuo Lin,Robert B Nussenblatt,Ryoichi Mori,Shawn M Burgess
View all publications
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