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AB82592

Anti-groEL antibody [9A1/2]

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(25 Publications)

Mouse Monoclonal Hsp60 antibody. Suitable for WB, IP and reacts with Recombinant fragment - Escherichia coli, Escherichia coli samples. Cited in 25 publications. Immunogen corresponding to Full Length Protein corresponding to Escherichia coli K-12 groEL.

View Alternative Names

groL, mopA, b4143, JW4103, groEL, Chaperonin GroEL, 60 kDa chaperonin, Chaperonin-60, GroEL protein, Cpn60, groL, mopA, Protein Cpn60, groEL protein, 60 kDa chaperonin

2 Images
Western blot - Anti-groEL antibody [9A1/2] (AB82592)
  • WB

Unknown

Western blot - Anti-groEL antibody [9A1/2] (AB82592)

This image was generated using the ascites version of the product.

All lanes:

Western blot - Anti-groEL antibody [9A1/2] (ab82592) at 1/1000 dilution

Lane 1:

groEL recombinant E. coli protein

Lane 2:

Hsp60 recombinant human protein (negative control)

Lane 3:

E. coli lysate

Predicted band size: 57 kDa

Observed band size: 57 kDa

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Western blot - Anti-groEL antibody [9A1/2] (AB82592)
  • WB

CiteAb

Western blot - Anti-groEL antibody [9A1/2] (AB82592)

groEL western blot using anti-groEL antibody [9A1/2] ab82592. Publication image and figure legend from Khodaparast, L., Khodaparast, L., et al., 2018, Nat Commun, PubMed 29491361.

ab82592 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab82592 please see the product overview.

Inclusion body formation and proteostatic collapse. a Growth curve of E. coli BL21-overexpressing p53CD (red) and control in the presence (green) or absence (blue) of P2 (average and SD of three replicates). p53CD bacterial growth in the presence of 0.4 mM IPTG. b Colony formation by E. coli BL21 p53CD-overexpressing bacteria. The bottom and top of the box are the first and third quartiles, and the band inside the box represents the median. The whiskers are drawn using Tukey’s method and show the extreme values that fall within 1.5 times the interquartile range. c Transmission electron microscopy image of an inclusion body from P2-treated E. coli O157 : H7 (uranyl acetate). d Representative Coomassie blue SDS-PAGE of inclusion bodies from E. coli BL21-overexpressing p53CD (lane 1), mock (lane 2), and E. coli O157 : H7 treated with P2 (lane 4), P2Pro (lane 5), or DMSO (lane 6). Molecular-weight markers are shown in lanes 3 and 7. e Western blot for dnaK, groEL, tig, and dnaJ of the same samples than that in d. f Fluorescence microscopy image of E. coli cells stably expressing a fluorescent fusion of DnaK (mCer) treated with P2 at MIC concentration. g Growth inhibition of cells treated with P2 with/without erythromycin (Erm, 100 μg/mL, average and SD of three replicates). h Percent of colony-forming units after treating bacterial KO strains (KEIO) for 1 h with P2 at its MIC concentration. i Percent of colony-forming units of chaperone-overexpressing E. coli strains treated by P2 peptide at MIC concentration for 1 h. Significant differences from the WT are calculated using ordinary one-way ANOVA and Dunnett’s multiple-comparison test. Statistical significance is indicated as follows : **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001

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Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

9A1/2

Isotype

IgG1

Carrier free

No

Reacts with

Escherichia coli

Applications

WB, IP

applications

Immunogen

Full Length Protein corresponding to Escherichia coli K-12 groEL. The exact immunogen used to generate this antibody is proprietary information.

P0A6F5

Reactivity data

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Product details

This product was changed from ascites to tissue culture supernatant on 22nd May 2019. Please note that the dilutions may need to be adjusted accordingly. If you have any questions, please do not hesitate to contact our scientific support team.

Properties and storage information

Form
Liquid
Purity
Tissue culture supernatant
Purification notes
Purified from TCS.
Storage buffer
Preservative: 0.09% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)
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 groEL protein often known as 60 kDa chaperonin is a highly conserved molecular chaperone with an approximate mass of 60 kilodaltons. It plays an integral role in assisting the correct folding of nascent or stress-denatured proteins in the cell. Expressed prominently in prokaryotic organisms such as E. coli groEL is an important component of the E. coli expression system due to its ability to maintain protein functionality. By forming a double-ring structure that encapsulates substrates groEL collaborates with its co-chaperonin groES to perform essential protein folding.
Biological function summary

GroEL functions in collaboration with groES as part of a chaperonin complex that stabilizes unfolded proteins and prevents aggregation. It operates by undergoing ATP-dependent conformational changes that create an environment conducive to proper protein folding. E. coli products such as enzymes and structural proteins rely on the folding mechanism orchestrated by groEL to achieve their native conformation. Consequently its role is indispensable for protein homeostasis within E. coli affecting diverse cellular processes.

Pathways

Molecular chaperones including groEL integrate into the protein quality control network which monitors and manages protein integrity and turnover. In particular groEL operates in the folding and stress response pathways. Working closely with other proteins such as DnaK and DnaJ groEL ensures efficient protein folding and repair especially during heat shock conditions. This function maintains cellular viability and is important for cellular adaptation to environmental stressors.

Disruptions in groEL function can lead to protein misfolding-related diseases like Alzheimer's and Parkinson's. Although direct links to groEL are less observed in eukaryotic systems similar chaperone proteins like HSP60 show connections to neurodegenerative disorders. Dysfunctional protein homeostasis due to insufficient chaperone activity highlights the role of molecular chaperones in preventing protein aggregation which is implicated in these diseases.

Product protocols

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

Target data

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed : 10532860, PubMed : 16751100, PubMed : 1676490, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391, PubMed : 2573517, PubMed : 2897629, PubMed : 8104102, PubMed : 9285593). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed : 16751100, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391). Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex (PubMed : 19915138, PubMed : 22445172, PubMed : 9285585, PubMed : 9285593). Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation (PubMed : 16684774, PubMed : 22445172, PubMed : 8861908, PubMed : 9285585). To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability (PubMed : 9285593). Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein (PubMed : 9285585, PubMed : 9285593). Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form (PubMed : 7867798, PubMed : 7915201). Can rescue kinetically trapped intermediates (PubMed : 20603018). GroEL shows ATPase activity (PubMed : 1676490, PubMed : 379350, PubMed : 9285593). ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding (PubMed : 9285593).. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.. (Microbial infection) Essential for the assembly of several bacteriophages.
See full target information groEL

Publications (25)

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

The FEBS journal 292:412-425 PubMed39658304

2024

Membrane anchoring of New Delhi metallo-β-lactamase-1 alters the fitness of Escherichia coli and increases its susceptibility to colistin by inducing outer membrane destabilization.

Applications

Unspecified application

Species

Unspecified reactive species

Bo Ma,Shan Zhou,Chao Fang,Mingzhi Wang,Xiaoyan Xue,Jianwei Xie,Jiayun Liu,Zheng Hou

The Journal of biological chemistry 300:107117 PubMed38403244

2024

The bacterial division protein MinDE has an independent function in flagellation.

Applications

Unspecified application

Species

Unspecified reactive species

Pinkilata Pradhan,Ashoka Chary Taviti,Tushar Kant Beuria

iScience 27:109101 PubMed38384838

2024

Mycobacterial Rv1804c binds to the PEST domain of IκBα and activates macrophage-mediated proinflammatory responses.

Applications

Unspecified application

Species

Unspecified reactive species

Jianjian Zheng,Chunsheng Dong,Sidong Xiong

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

Gut microbes 16:2316932 PubMed38356294

2024

serovar Typhimurium remodels mitochondrial dynamics of macrophages via the T3SS effector SipA to promote intracellular proliferation.

Applications

Unspecified application

Species

Unspecified reactive species

Xingmei Liu,Yutao Liu,Xinyu Zhao,Xueping Li,Ting Yao,Ruiying Liu,Qian Wang,Qiushi Wang,Dan Li,Xintong Chen,Bin Liu,Lu Feng

International journal of molecular sciences 24: PubMed38139044

2023

Phosphate (Pi) Transporter PIT1 Induces Pi Starvation in -Containing Vacuole in HeLa Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Wen Yang,Yingxing Feng,Jun Yan,Chenbo Kang,Ting Yao,Hongmin Sun,Zhihui Cheng

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 10:e2303911 PubMed37698584

2023

Black Phosphorus/MnO Nanocomposite Disrupting Bacterial Thermotolerance for Efficient Mild-Temperature Photothermal Therapy.

Applications

Unspecified application

Species

Unspecified reactive species

Feng Wang,Qinghe Wu,Guoping Jia,Lingchi Kong,Rongtai Zuo,Kai Feng,Mengfei Hou,Yimin Chai,Jia Xu,Chunfu Zhang,Qinglin Kang

Frontiers in cellular and infection microbiology 12:1014897 PubMed36439208

2022

Mycobacterium tuberculosis Rv0790c inhibits the cellular autophagy at its early stage and facilitates mycobacterial survival.

Applications

Unspecified application

Species

Unspecified reactive species

Jun Fang,Chunsheng Dong,Sidong Xiong

Nature 596:597-602 PubMed34408320

2021

Molecular basis for DarT ADP-ribosylation of a DNA base.

Applications

Unspecified application

Species

Unspecified reactive species

Marion Schuller,Rachel E Butler,Antonio Ariza,Callum Tromans-Coia,Gytis Jankevicius,Tim D W Claridge,Sharon L Kendall,Shan Goh,Graham R Stewart,Ivan Ahel

Cell reports 36:109413 PubMed34289355

2021

A dynamic and multilocus metabolic regulation strategy using quorum-sensing-controlled bacterial small RNA.

Applications

Unspecified application

Species

Unspecified reactive species

Shao-Heng Bao,Hui Jiang,Ling-Yun Zhu,Ge Yao,Peng-Gang Han,Xiu-Kun Wan,Kang Wang,Tian-Yu Song,Chang-Jun Liu,Shan Wang,Zhe-Yang Zhang,Dong-Yi Zhang,Er Meng
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