GrpE E.Coli

The HSP-70 Cofactor (HSP24) E.Coli Recombinant, also known as GrpE, is a crucial protein in the cellular stress response system of Escherichia coli (E. coli). This protein plays a significant role in the heat shock response, which is a universal mechanism that cells employ to cope with elevated temperatures and other stress conditions.

GrpE is a single, non-glycosylated polypeptide chain consisting of 197 amino acids and has a molecular mass of approximately 21.8 kDa . The recombinant form of this protein is produced in E. coli and is purified using proprietary chromatographic techniques to ensure high purity and functionality .

GrpE functions as a co-chaperone in association with the DnaK-DnaJ chaperone system. This system is essential for the proper folding of proteins, especially under stress conditions. GrpE acts as a nucleotide exchange factor for DnaK, facilitating the release of ADP and the binding of ATP, which is a critical step in the chaperone cycle .

One of the unique features of GrpE is its potential role as a thermosensor. It actively participates in the response to hyperosmotic and heat shock conditions by preventing the aggregation of stress-denatured proteins . Several rounds of ATP-dependent interactions between DnaJ, DnaK, and GrpE are required for fully efficient protein folding .

The heat shock response is vital for cell survival under stress conditions. GrpE, as part of the HSP-70 chaperone system, helps maintain protein homeostasis by ensuring that proteins fold correctly and do not aggregate. This function is particularly important in environments where cells are exposed to fluctuating temperatures and other stressors .

Recombinant GrpE produced in E. coli is widely used in research to study protein folding mechanisms, stress responses, and the role of chaperone systems in cellular biology. Its high purity and functionality make it a valuable tool for biochemical and biophysical studies .