Recombinant E. coli GrpE protein
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(1 Publication)
Recombinant E. coli GrpE protein is a Escherichia coli K-12 Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
b2614, JW2594, grpE, Protein GrpE, HSP-70 cofactor, HSP24, Heat shock protein B25.3
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant E. coli GrpE protein (AB63839)
3μg protein in 15% SDS-PAGE.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
GrpE acts as a nucleotide exchange factor within the chaperone system specifically with DnaK and DnaJ proteins. GrpE facilitates the release of ADP from DnaK allowing ATP binding and subsequent release of the substrate protein. This process is central to the correct folding and repair of proteins that may become misfolded or denatured. GrpE DnaK and DnaJ form a chaperone complex that is essential for protein quality control and cellular functions.
Pathways
GrpE serves a significant role in bacterial heat shock response pathways and proteostasis. It is integrally associated with the Hsp70/DnaK protein folding pathway which is vital in dealing with cellular stress and maintaining protein integrity. GrpE interacts directly with DnaK and indirectly through the DnaJ co-chaperone forming an important triad for bacterial survival under various stress conditions such as elevated temperatures.
Specifications
Form
Liquid
Additional notes
ab63839 was overexpressed in E.coli and purified by using the conventional column chromatography techniques.
General info
Function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Sequence similarities
Belongs to the GrpE family.
Target data
Publications (1)
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Molecular cell 70:614-627.e7 PubMed29754824
2018
Applications
Unspecified application
Species
Unspecified reactive species
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