GroES Human, His
Description
Product Specs
Product Science Overview
GroES, also known as Heat Shock Protein 10 (HSP10), is a molecular chaperone that plays a crucial role in protein folding under both normal and stress conditions. It is part of the chaperonin family, which includes proteins that assist in the proper folding of other proteins. GroES specifically interacts with another chaperonin, HSP60, to facilitate the correct folding of polypeptides.
GroES is a small protein with a molecular weight of approximately 10 kDa. It consists of 102 amino acids and is characterized by its ability to form a heptameric ring structure. This ring structure is essential for its function as a chaperone. The recombinant form of GroES, tagged with a His (histidine) tag, is often used in research to facilitate purification and detection.
The primary function of GroES is to bind to HSP60 in the presence of adenosine triphosphate (ATP). This binding induces a conformational change in HSP60, creating an enclosed environment where protein folding can occur. The hydrolysis of ATP by HSP60 destabilizes the GroES-HSP60 complex, allowing the folded protein to be released .
Recombinant GroES (HSP10) is typically produced in Escherichia coli (E. coli) expression systems. The gene encoding GroES is cloned into an expression vector, which is then introduced into E. coli cells. These cells are cultured under conditions that induce the expression of the recombinant protein. The His tag attached to GroES allows for easy purification using affinity chromatography techniques, such as nickel-nitrilotriacetic acid (Ni-NTA) chromatography .
Recombinant GroES (HSP10) is widely used in biochemical and biophysical studies to understand protein folding mechanisms. It is also employed in the production of recombinant proteins, where it helps to ensure proper folding and stability. Additionally, GroES is used in studies related to stress responses and cellular homeostasis.
Recombinant GroES (HSP10) is typically supplied as a lyophilized powder or in a sterile-filtered solution. It should be stored at -20°C for long-term storage. After reconstitution, it can be stored at 4°C for short periods. To avoid repeated freeze-thaw cycles, aliquoting the reconstituted protein is recommended .
