JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB69823

Anti-groES antibody

Be the first to review this product! Submit a review

|

(5 Publications)

Rabbit Polyclonal EPF antibody. Suitable for IP, WB and reacts with Escherichia coli, Recombinant full length protein - Escherichia coli samples. Cited in 5 publications.
1 Images
Western blot - Anti-groES antibody (AB69823)
  • WB

Unknown

Western blot - Anti-groES antibody (AB69823)

All lanes:

Western blot - Anti-groES antibody (ab69823) at 1/5000 dilution

Lane 1:

Molecular weight marker

Lane 2:

groES recombinant E. coli protein

Lane 3:

No lysates (empty)

Lane 4:

Lysates prepared from E.coli

Predicted band size: 11 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Escherichia coli

Applications

IP, WB

applications

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Escherichia coli": { "IP-species-checked": "guaranteed", "IP-species-dilution-info": "1/200", "IP-species-notes": "<p></p>", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Recombinant full length protein - Escherichia coli": { "IP-species-checked": "notRecommended", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/5000", "WB-species-notes": "<p>for colorimetric detection. 1/500 for ECL.</p>" } } }

Properties and storage information

Form
Liquid
Purity
Whole antiserum
Storage buffer
Constituents: Whole serum
Shipped at conditions
Blue Ice
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 information

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

The groES protein also known as Hsp10 plays a mechanical role as a molecular chaperone. It partners with the groEL protein to facilitate the correct folding of other proteins. The groES protein has a mass of approximately 10 kDa and is universally expressed across a wide range of species from prokaryotes to eukaryotes. It comprises a heptameric ring structure that caps the groEL complex making it critical in the chaperonin cycle. groES specifically binds to the groEL protein assisting in the folding of unfolded or misfolded substrates within the cellular environment.
Biological function summary

The groES protein functions within a chaperonin complex alongside groEL to prevent aggregation and promote proper protein folding. This complex plays a significant role in cellular stress response and stabilization of proteins especially under heat shock conditions. The chaperonin system refolds denatured proteins and maintains proteostasis ensuring efficient cellular function. The groES and groEL interaction facilitates timed ATP hydrolysis which is necessary for the release of correctly folded proteins back into the cellular environment.

Pathways

GroES integrates into cellular stress response and protein quality control pathways. It is important in the protein processing pathway alongside groEL and Hsp70 enabling effective folding of nascent polypeptides. GroES and these chaperones serve as emergency machinery to protect the cell during adverse conditions such as thermal or oxidative stress. Together they prevent cellular damage caused by protein misfolding which may otherwise lead to cytotoxicity or cell death.

The groES protein has connections to various pathologies linked to protein misfolding and aggregation such as neurodegenerative diseases. Specifically its function relates to conditions like Alzheimer's and Parkinson's disease where protein folding malfunctions play an important role. The interaction between groES and proteins like groEL and Hsp70 is pivotal in preventing the accumulation of misfolded protein aggregates associated with these disorders. Targeting the chaperonin system has become a potential strategy in managing diseases where maintaining proteostasis mitigates cellular dysfunction.

Product protocols

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

Publications (5)

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

RNA biology 21:1-18 PubMed38361426

2024

RNA-dependent proteome solubility maintenance in lysates analysed by quantitative mass spectrometry: Proteomic characterization in terms of isoelectric point, structural disorder, functional hub, and chaperone network.

Applications

Unspecified application

Species

Unspecified reactive species

Chan Park,Bitnara Han,Yura Choi,Yoontae Jin,Kwang Pyo Kim,Seong Il Choi,Baik L Seong

Pharmaceuticals (Basel, Switzerland) 14: PubMed34959736

2021

Effect of Plasmonic Gold Nanoprisms on Biofilm Formation and Heat Shock Proteins Expression in Human Pathogenic Bacteria.

Applications

Unspecified application

Species

Unspecified reactive species

Rihab Lagha,Fethi Ben Abdallah,Amine Mezni,Othman M Alzahrani

Molecular biology and evolution 32:2681-93 PubMed26116858

2015

Fitness Trade-Offs Determine the Role of the Molecular Chaperonin GroEL in Buffering Mutations.

Applications

Unspecified application

Species

Unspecified reactive species

Beatriz Sabater-Muñoz,Maria Prats-Escriche,Roser Montagud-Martínez,Adolfo López-Cerdán,Christina Toft,José Aguilar-Rodríguez,Andreas Wagner,Mario A Fares

Molecular microbiology 89:715-31 PubMed23802546

2013

Differential control of Salmonella heat shock operons by structured mRNAs.

Applications

Unspecified application

Species

Unspecified reactive species

Annika Cimdins,Johanna Roßmanith,Sina Langklotz,Julia E Bandow,Franz Narberhaus

Journal of proteomics 75:511-6 PubMed21889622

2011

iTRAQ-coupled 2-D LC-MS/MS analysis of cytoplasmic protein profile in Escherichia coli incubated with apidaecin IB.

Applications

WB

Species

Escherichia coli

Yusi Zhou,Wei Ning Chen
View all publications

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com