Abcam, ab113176, Recombinant E. coli groEL protein

Size: 50µg
Recombinant E. coli groEL protein is a Escherichia coli CFT073 Full Length protein, in the 2 to 548 aa range, expressed in Escherichia coli, with >90%, suitable for ELISA, EIA, WB, FuncS.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:FuncS, ELISA, WB, EIASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:P0A6F6,
Animal free:No,
Carrier free:No,
Species:Escherichia coli CFT073,
Storage buffer:Preservative: 0.05% Sodium azideConstituents: 0.79% Tris HCl, 0.58% Sodium chloride, 0.1% Magnesium chloride, 0.08% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°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.