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AB53109

Anti-Hsp60 antibody - Mitochondrial Marker

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(8 Publications)

Rabbit Polyclonal Hsp60 antibody. Suitable for WB, IHC-P, ICC/IF and reacts with Human samples. Cited in 8 publications. Immunogen corresponding to Synthetic Peptide within Human HSPD1 aa 500 to C-terminus.

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

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-Hsp60 antibody - Mitochondrial Marker (AB53109)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-Hsp60 antibody - Mitochondrial Marker (AB53109)

ICC/IF image of ab53109 stained HeLa cells. The cells were 100% methanol fixed (5 min) and then incubated in 1%BSA / 10% normal goat serum / 0.3M glycine in 0.1% PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated with the antibody (ab53109, 1µg/ml) overnight at +4°C. The secondary antibody (green) was Alexa Fluor® 488 goat anti-rabbit IgG (H+L) used at a 1/1000 dilution for 1h. Alexa Fluor® 594 WGA was used to label plasma membranes (red) at a 1/200 dilution for 1h. DAPI was used to stain the cell nuclei (blue) at a concentration of 1.43µM.

Western blot - Anti-Hsp60 antibody - Mitochondrial Marker (AB53109)
  • WB

Unknown

Western blot - Anti-Hsp60 antibody - Mitochondrial Marker (AB53109)

All lanes:

Western blot - Anti-Hsp60 antibody - Mitochondrial Marker (ab53109) at 1/300 dilution

Lane 1:

extract from COLO205 cells

Lane 2:

extract from COLO205 cells with immunising peptide

Predicted band size: 61 kDa

Observed band size: 60 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, ICC/IF, WB

applications

Immunogen

Synthetic Peptide within Human HSPD1 aa 500 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

P10809

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

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.

Product protocols

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

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

Publications (8)

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

NPJ Parkinson's disease 10:80 PubMed38594264

2024

Elevated α-synuclein levels inhibit mitophagic flux.

Applications

Unspecified application

Species

Unspecified reactive species

Inge Kinnart,Liselot Manders,Thibaut Heyninck,Dorien Imberechts,Roman Praschberger,Nils Schoovaerts,Catherine Verfaillie,Patrik Verstreken,Wim Vandenberghe

Molecular medicine (Cambridge, Mass.) 29:57 PubMed37095454

2023

ATF5 regulates tubulointerstitial injury in diabetic kidney disease via mitochondrial unfolded protein response.

Applications

Unspecified application

Species

Unspecified reactive species

Yifei Liu,Lei Zhang,Shumin Zhang,Jialu Liu,Xiaohui Li,Kexin Yang,Danyi Yang,Yu Liu,Lin Sun,Fuyou Liu,Li Xiao

Genes 13: PubMed36553628

2022

A Patient with Corticobasal Syndrome and Progressive Non-Fluent Aphasia (CBS-PNFA), with Variants in , , , and Genes.

Applications

Unspecified application

Species

Unspecified reactive species

Katarzyna Gaweda-Walerych,Emilia J Sitek,Małgorzata Borczyk,Ewa Narożańska,Bogna Brockhuis,Michał Korostyński,Michał Schinwelski,Mariusz Siemiński,Jarosław Sławek,Cezary Zekanowski

Brain : a journal of neurology 145:4368-4384 PubMed36039535

2022

DJ-1 is an essential downstream mediator in PINK1/parkin-dependent mitophagy.

Applications

Unspecified application

Species

Unspecified reactive species

Dorien Imberechts,Inge Kinnart,Fieke Wauters,Joanne Terbeek,Liselot Manders,Keimpe Wierda,Kristel Eggermont,Rodrigo Furtado Madeiro,Carolyn Sue,Catherine Verfaillie,Wim Vandenberghe

Human molecular genetics 29:1096-1106 PubMed32068847

2020

CHCHD2 harboring Parkinson's disease-linked T61I mutation precipitates inside mitochondria and induces precipitation of wild-type CHCHD2.

Applications

Unspecified application

Species

Unspecified reactive species

Tom Cornelissen,Marco Spinazzi,Shaun Martin,Dorien Imberechts,Peter Vangheluwe,Matthew Bird,Bart De Strooper,Wim Vandenberghe

Autophagy 16:203-222 PubMed30945962

2019

mutations impair depolarization-induced mitophagy through inhibition of mitochondrial accumulation of RAB10.

Applications

Unspecified application

Species

Unspecified reactive species

Fieke Wauters,Tom Cornelissen,Dorien Imberechts,Shaun Martin,Brianada Koentjoro,Carolyn Sue,Peter Vangheluwe,Wim Vandenberghe

Scientific reports 6:19781 PubMed26812922

2016

Skeletal muscle Heat shock protein 60 increases after endurance training and induces peroxisome proliferator-activated receptor gamma coactivator 1 α1 expression.

Applications

Unspecified application

Species

Unspecified reactive species

Rosario Barone,Filippo Macaluso,Claudia Sangiorgi,Claudia Campanella,Antonella Marino Gammazza,Viviana Moresi,Dario Coletti,Everly Conway de Macario,Alberto Jl Macario,Francesco Cappello,Sergio Adamo,Felicia Farina,Giovanni Zummo,Valentina Di Felice

Analytical biochemistry 418:213-23 PubMed21820998

2011

Isolation of functional mitochondria from rat kidney and skeletal muscle without manual homogenization.

Applications

WB

Species

Rat

Vera S Gross,Heather K Greenberg,Sergei V Baranov,Greta M Carlson,Irina G Stavrovskaya,Alexander V Lazarev,Bruce S Kristal
View all publications

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