DnaK is the prokaryotic analogue of eukaryotic Hsp70, a member of the heat shock proteins. It assists the protein assembly, folding, and translocation.
The bacterial chaperonin GroEL is a double toroidal assembly, which together with the action of the ring-shaped oligomeric cochaperonin, GroES, facilitates protein folding in an ATP dependent manner.
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 overexpressed 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 has a 6His-tag at N-terminus and is purified by proprietary chromatographic techniques.
