GroES E.Coli

GroES is a small protein with a molecular weight of approximately 10 kDa. It exists as a ring-shaped oligomer composed of six to eight identical subunits . The primary function of GroES is to bind to GroEL in the presence of ATP, causing a conformational change in GroEL. This change encloses the protein substrate within the GroEL-GroES complex, providing an isolated environment for the protein to fold correctly .

The binding of GroES to GroEL inhibits the weak ATPase activity of GroEL. ATP hydrolysis by GroEL destabilizes the GroEL-GroES complex, allowing it to dissociate and release the properly folded protein .

Recombinant GroES (HSP10) is produced in E. coli as a single, non-glycosylated polypeptide chain containing 102 amino acids . The recombinant protein is purified using proprietary chromatographic techniques to achieve a purity greater than 98%, as determined by SDS-PAGE and RP-HPLC .

Recombinant GroES (HSP10) is used in various research applications, including studies on protein folding, chaperone function, and stress response mechanisms. It is also utilized in the production of recombinant proteins, where it helps ensure proper folding and stability of the target proteins.

Recombinant GroES (HSP10) should be stored at 4°C if it will be used within 2-4 weeks. For longer storage periods, it should be stored at or below -20°C. The addition of a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), is recommended for long-term storage .