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
- WB
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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
true
- 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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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
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Publications (25)
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The FEBS journal 292:412-425 PubMed39658304
2024
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The Journal of biological chemistry 300:107117 PubMed38403244
2024
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iScience 27:109101 PubMed38384838
2024
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RNA biology 21:1-18 PubMed38361426
2024
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Gut microbes 16:2316932 PubMed38356294
2024
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International journal of molecular sciences 24: PubMed38139044
2023
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Advanced science (Weinheim, Baden-Wurttemberg, Germany) 10:e2303911 PubMed37698584
2023
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Frontiers in cellular and infection microbiology 12:1014897 PubMed36439208
2022
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Nature 596:597-602 PubMed34408320
2021
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Cell reports 36:109413 PubMed34289355
2021
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