Anti-groEL antibody [9A1/2],Abcam,AB82592

This product was changed from ascites to tissue culture supernatant on 22 nd 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.

Host

Mouse

Reactivity

Escherichia coli

Application

WB, IP

Platform ID

BAB199426052

Abcam

Headquarters

Discovery Drive Cambridge Biomedical Campus Cambridge CB2 0AX UK

Contact

Tel: +44 (0)1223 696000
Fax: +44 (0)1223 215 215

Product Specifications
Scientific Background

Specifications

NameAnti-groEL antibody [9A1/2]
Cat. No.AB82592
HostMouse
IsotypeIgG1
ReactivityEscherichia coli
ApplicationWB, IP
ClonalityMonoclonal
Clone Number9A1/2
ImmunogenFull Length Protein corresponding to Escherichia coli K-12 groEL. The exact immunogen used to generate this antibody is proprietary information.
Appearance/FormLiquid
ShippingBlue Ice
FormulationPreservative: 0.09% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Storage-20°C
Regulatory StatusResearch Use Only

Scientific Background

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

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