Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
PDI Human Recombinant produced in E.Coli is a 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.
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