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Redox Environment Supplements Promote Disulfide Bond Formation Formation of disulfide bonds is important for folding and stability of secretory proteins such as enzymes or antibodies. Disulfide bonds are usually formed by oxidation of sulfhydryl groups (SH-) of adjacent cysteine residues. Therefore, disulfide bond formation efficiency depends on redox state. Additionally, disulfide bond isomerase which can catalyze the exchange of disulfide bridges may be required for correct cysteine pairing.
Redox Supplement

DsbC Set comprises highly purified
E. coli DsbC (a disulfide bond isomerase) which can catalyze disulfide bridge exchange, and GSSG (oxidized Glutathione) to enforce an oxidized environment.
Redox Supplement
PDI Set comprises oxidized glutathione (GSSG), human PDI (protein disulfide isomerase) and human Ero1α (ER oxidoreductin-1 to reoxidize PDI).