Mouse Monoclonal Hsp60 antibody. Suitable for WB, IP and reacts with Recombinant fragment - Escherichia coli, Escherichia coli samples. Cited in 19 publications. Immunogen corresponding to Full Length Protein corresponding to Escherichia coli K-12 groEL.
Images
![Western blot - Anti-groEL antibody [9A1/2] (AB82592), expandable thumbnail](https://content.abcam.com/products/images/groel-antibody-9a1-2-ab82592--western-blot-img28173.jpg/_jcr_content/renditions/webp-475.webp "Western blot - Anti-groEL antibody [9A1/2] (AB82592)")
![Western blot - Anti-groEL antibody [9A1/2] (AB82592), expandable thumbnail](https://content.abcam.com/products/images/groel-antibody-9a1-2-ab82592--western-blot-img442800.jpg/_jcr_content/renditions/webp-475.webp "Western blot - Anti-groEL antibody [9A1/2] (AB82592)")
Publications
Filter by
- International journal of molecular sciences 24:2023Phosphate (Pi) Transporter PIT1 Induces Pi Starvation in -Containing Vacuole in HeLa Cells.Applications:Unspecified applicationReactive species:Unspecified reactive speciesWen Yang,Yingxing Feng,Jun Yan,Chenbo Kang,Ting Yao,Hongmin Sun,Zhihui ChengPubMed 38139044
- Frontiers in cellular and infection microbiology 12:10148972022Mycobacterium tuberculosis Rv0790c inhibits the cellular autophagy at its early stage and facilitates mycobacterial survival.Applications:Unspecified applicationReactive species:Unspecified reactive speciesJun Fang,Chunsheng Dong,Sidong XiongPubMed 36439208
- Nature 596:597-6022021Molecular basis for DarT ADP-ribosylation of a DNA base.Applications:Unspecified applicationReactive species:Unspecified reactive speciesMarion Schuller,Rachel E Butler,Antonio Ariza,Callum Tromans-Coia,Gytis Jankevicius,Tim D W Claridge,Sharon L Kendall,Shan Goh,Graham R Stewart,Ivan AhelPubMed 34408320
- Cell reports 36:1094132021A dynamic and multilocus metabolic regulation strategy using quorum-sensing-controlled bacterial small RNA.Applications:Unspecified applicationReactive species:Unspecified reactive speciesShao-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 MengPubMed 34289355
- Journal of bacteriology 203:e00143212021Low Cytoplasmic Magnesium Increases the Specificity of the Lon and ClpAP Proteases.Applications:Unspecified applicationReactive species:Unspecified reactive speciesJinki Yeom,Eduardo A GroismanPubMed 33941609
- mBio 11:2020Magnesium Sensing Regulates Intestinal Colonization of Enterohemorrhagic Escherichia coli O157:H7.Applications:Unspecified applicationReactive species:Unspecified reactive speciesYutao Liu,Runhua Han,Junyue Wang,Pan Yang,Fang Wang,Bin YangPubMed 33173003
- Proceedings of the National Academy of Sciences of 117:20235-202432020Small proteins regulate survival inside macrophages by controlling degradation of a magnesium transporter.Applications:Unspecified applicationReactive species:Unspecified reactive speciesJinki Yeom et. al.PubMed 32753384
- eLife 9:2020Hfq CLASH uncovers sRNA-target interaction networks linked to nutrient availability adaptation.Applications:Unspecified applicationReactive species:Unspecified reactive speciesIra Alexandra Iosub et. al.PubMed 32356726
- Nature communications 10:35172019The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase.Applications:Unspecified applicationReactive species:Unspecified reactive speciesBo Ma,Chao Fang,Linshan Lu,Mingzhi Wang,Xiaoyan Xue,Ying Zhou,Mingkai Li,Yue Hu,Xiaoxing Luo,Zheng HouPubMed 31388008
- International immunopharmacology 73:64-712019Plasma membrane localization of CYP4Z1 and CYP19A1 and the detection of anti-CYP19A1 autoantibodies in humans.Applications:Unspecified applicationReactive species:Unspecified reactive speciesChristopher Khayeka-Wandabwa et. al.PubMed 31082724
Key facts
- Isotype
- IgG1
- Host species
- Mouse
- Storage buffer
Preservative: 0.09% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine)- Form
- Liquid
- Clonality
- Monoclonal
Immunogen
- Full Length Protein corresponding to Escherichia coli K-12 groEL. The exact immunogen used to generate this antibody is proprietary information. Database link P0A6F5
Reactivity data
Select an application| WB | IP | |
|---|---|---|
| Escherichia coli | Tested | Expected |
| Recombinant fragment - Escherichia coli | Tested | Not recommended |
WB
TestedTested
| Species | Dilution info | Notes |
|---|---|---|
Species Recombinant fragment - Escherichia coli, Escherichia coli | Dilution info - | Notes - |
IP
ExpectedExpected
| Species | Dilution info | Notes |
|---|---|---|
Species Escherichia coli | Dilution info Use at an assay dependent concentration. | Notes - |
Not recommendedNot recommended
| Species | Dilution info | Notes |
|---|---|---|
Species Recombinant fragment - Escherichia coli | Dilution info - | Notes - |
Associated Products
Select an associated product type
1 product for Alternative Product
Target data
Function
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.
Additional Targets
groEL
Alternative names
groL, mopA, b4143, JW4103, groEL, Chaperonin GroEL, 60 kDa chaperonin, Chaperonin-60, GroEL protein, Cpn60
Recommended products
Mouse Monoclonal Hsp60 antibody. Suitable for WB, IP and reacts with Recombinant fragment - Escherichia coli, Escherichia coli samples. Cited in 19 publications. Immunogen corresponding to Full Length Protein corresponding to Escherichia coli K-12 groEL.
Key facts
- Isotype
- IgG1
- Host species
- Mouse
- Storage buffer
Preservative: 0.09% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine)- Form
- Liquid
- Clonality
- Monoclonal
- Immunogen
- Full Length Protein corresponding to Escherichia coli K-12 groEL. The exact immunogen used to generate this antibody is proprietary information. Database link P0A6F5
- Clone number
- 9A1/2
- Purity
- Tissue culture supernatant
- Concentration
- Purification notes
Purified from TCS.
Storage
- 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
Notes
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.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
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.
- Associated diseases and disorders
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 promise
Tested
We have tested this species and application combination and it works. It is covered by our product promise.
Expected
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
Predicted
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
Not recommended
We do not recommend this combination. It is not covered by our product promise.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
2 product images
![Western blot - Anti-groEL antibody [9A1/2] (ab82592), expandable thumbnail](https://content.abcam.com/products/images/groel-antibody-9a1-2-ab82592--western-blot-img28173.jpg "Western blot - Anti-groEL antibody [9A1/2] (ab82592)")
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
Developed using the ECL technique.
Predicted band size: 57 kDa
Observed band size: 57 kDa
![Western blot - Anti-groEL antibody [9A1/2] (ab82592), expandable thumbnail](https://content.abcam.com/products/images/groel-antibody-9a1-2-ab82592--western-blot-img442800.jpg "Western blot - Anti-groEL antibody [9A1/2] (ab82592)")
Image collected and cropped by CiteAb under a CC-BY license from the publication
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
Downloads
Product protocols
- Visit the general protocols
- Visit troubleshooting
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