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GroEL (E. coli) polyclonal antibody

ADI-SPS-875

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GroEL and GroES are E. coli chaperonins, which are homologs of mitochondrial chaperonins Hsp60 and Hsp10. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding with an ATP-dependent mechanism.

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This antibody is covered by our Worry-Free Guarantee.

GroEL (E. coli) polyclonal antibody Western blot — Western Blot Analysis of GroEL: Lane 1: MW Marker, Lane 2: GroEL (E. coli), (recombinant) (Prod. No. ADI-SPP-610), Lane 3: HSP60 (human), (recombinant) (Prod. No. ADI-NSP-540), Lane 4: HeLa (Heat Shocked), Cell Lysate (Prod. No. ADI-LYC-HL101), Lane 5: E. coli Cell Lysate all probed with GroEL (E. coli), pAb (Prod. No. ADI-SPS-875).

Product Details

Alternative Name	Chaperonin 60
Application	WB
Application Notes	Detects a band of ~60kDa by Western blot.
Formulation	Liquid. In PBS containing 50% glycerol and 0.09% sodium azide.
Host	Rabbit
Immunogen	E. coli GroEL.
Purity Detail	Protein A affinity purified.
Recommendation Dilutions/Conditions	Western Blot (1:1,000, colorimetric)Suggested dilutions/conditions may not be available for all applications.Optimal conditions must be determined individually for each application.
Source	Purified from rabbit serum.
Species Reactivity	E. coli
UniProt ID	P0A6F5 (strain K12)
Worry-free Guarantee	This antibody is covered by our Worry-Free Guarantee.

Handling & Storage

Handling	Avoid freeze/thaw cycles.
Long Term Storage	-20°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

Shigella flexneri evades LPS ubiquitylation through IpaH1.4-mediated degradation of RNF213: Naydenova, K., Boyle, K. B., et al.; Nat. Struct. Mol. Biol. , (2025), Abstract
The discovery and structural basis of two distinct state-dependent inhibitors of BamA: D. Sun, et al.; Nat. Commun. 15, 8718 (2024), Abstract
Shigella flexnerievades LPS ubiquitylation through IpaH1.4-mediated degradation of RNF213: Naydenova, K., Boyle, K. B., et al.; bioRxiv , (2024)
Function of the bacteriophage P2 baseplate central spike Apex domain in the infection process: J.M. Miller, et akl.; bioRxiv , (2023), Application(s): WB, Abstract
Mycobacterial chaperonins in cellular proteostasis: Evidence for chaperone function of Cpn60.1 and Cpn60.2-mediated protein folding: Piplani, B., Kumar, C. M. S., et al.; Mol. Microbiol. 120, 210 (2023), Abstract
Mycobacterium abscessus HelR interacts with RNA polymerase to confer intrinsic rifamycin resistance: Hurst-Hess, K. R., Saxena, A., et al.; Mol. Cell 82, 3166 (2022), Abstract
Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection: Otten, E. G., Werner, E., et al.; Nature 594, 111 (2021), Abstract
A Bacterial Effector Mimics a Host HSP90 Client to Undermine Immunity.: Tagliabracci, V. S., Tomchick, D. R., et al.; Cell 179, 205 (2019), Application(s): WB, Abstract
Protein AMPylation by an Evolutionarily Conserved Pseudokinase: A. Sreelatha, et al.; Cell 175, 809 (2018), Abstract
The Bradyrhizobium japonicum ferrous iron transporter FeoAB is required for ferric iron utilization in free-living aerobic cells and for symbiosis: S. Sankari, et al.; J. Biol. Chem. 291, 15653 (2016), Application(s): Western-blot, Abstract — Full Text

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GroEL (E. coli) polyclonal antibody

ADI-SPS-875

Product Details

Handling & Storage

Datasheet, Manuals, SDS & CofA

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