GroEL protein is a member of the chaperonin family that is required for proper protein folding. GroEL consists of 14 subunits with a total molecular weight of 57.3kDA. The recombinant full length protein was overexpressed in E.coli and purified by chromatography.
GroES protein is a chaperonin family protein that works in conjunction with GroEL to facilitate proper protein folding. GroES consists of 7 subunits with a molecular weight of 10.4kDA. The recombinant full length protein was overexpression in E.coli and purified by chromatography.
Recombinant yeast PDI is produced in E.Coli is as single, non-glycosylated, polypeptide chain containing 503 amino acids and having a molecular mass of 62.4 kDa. The PDI is fused to a 12 amino acid His tag (515 a.a. total) at N-terminal and purified by proprietary chromatographic techniques.
