Recombinant E. coli GrpE protein is a Escherichia coli K-12 Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
M S S K E Q K T P E G Q A P E E I I M D Q H E E I E A V E P E A S A E Q V D P R D E K I A N L E A Q L A E A Q T R E R D G I L R V K A E M E N L R R R T E L D I E K A H K F A L E K F I N E L L P V I D S L D R A L E V A D K A N P D M S A M V E G I E L T L K S M L D V V R K F G V E V I A E T N V P L D P N V H Q A I A M V E S D D V A P G N V L G I M Q K G Y T L N G R T I R A A M V T V A K A K A
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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.
GrpE
b2614, JW2594, grpE, Protein GrpE, HSP-70 cofactor, HSP24, Heat shock protein B25.3
Recombinant E. coli GrpE protein is a Escherichia coli K-12 Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 0.58% Sodium chloride, 0.242% Tris
ab63839 was overexpressed in E.coli and purified by using the conventional column chromatography techniques.
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.
Belongs to the GrpE family.
The GrpE protein also known simply as GrpE functions as a molecular chaperone and co-chaperone in bacteria assisting in protein folding and repair by helping the Hsp70 chaperone system. It is encoded by the grpE gene. GrpE has an approximate molecular mass of 21 kDa. This protein is mainly expressed in the cytoplasm of bacterial cells where it plays a significant role in maintaining protein homeostasis under stress conditions such as heat shock. GrpE acts synergistically with DnaK another essential component of the bacterial chaperone machinery.
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.
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.
GrpE and its associated chaperone complex have relevance in pathogenic bacteria contributing to their virulence and infection capability. For example GrpE in Escherichia coli is implicated in increased virulence supporting bacterial resistance to environmental stressors. This protein complex might interact with various bacterial virulence factors and stress proteins that could amplify the pathogen's ability to survive hostile environments such as within a host organism's immune response.
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3μg protein in 15% SDS-PAGE.
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