GroEL Human

Recombinant Human GroEL (HSP60) is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain. It is fused to a 20 amino acid His tag at the N-terminus, containing a total of 593 amino acids (1-573 a.a.) and has a molecular mass of approximately 63 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity, typically greater than 95% as determined by SDS-PAGE .

GroEL (HSP60) functions as a molecular chaperone, assisting in the proper folding of proteins within the mitochondrial matrix. It is regulated by the cochaperonin HSP10 (GroES), which forms a unique complex with HSP60. HSP10 is a single heptameric protein ring with a molecular mass of 10 kDa . This complex coordinates the ATPase activity of the HSP60 subunits, facilitating the release of bound polypeptides in a manner that promotes correct folding .

The role of GroEL (HSP60) is vital in various cellular processes, particularly under conditions of environmental and pathophysiological stress. The synthesis of heat shock proteins, including HSP60, is triggered by a wide variety of stressful conditions, making them essential for cellular protection and recovery .

Recombinant Human GroEL (HSP60) is widely used in research for studying protein folding, mitochondrial function, and stress response mechanisms. It is also utilized in various biochemical assays and experiments to understand its role in cellular homeostasis and protein management.

For optimal stability, GroEL (HSP60) should be stored at 4°C if used within 2-4 weeks. For longer storage periods, it is recommended to freeze the protein at -20°C, preferably with a carrier protein such as 0.1% HSA or BSA to avoid multiple freeze-thaw cycles .