Description
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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.
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Reagent Qty Description Storage GSSG 12.5 ul Oxidized glutathione (60 mM) -20 C DSBC 25 ul E.coli DsbC (320 µM *2) (No tags) -80 C Dilution Buffer 500ul 30% glycerol buffer -20 C
Redox Supplement
PDI Set comprises oxidized glutathione (GSSG), human PDI (protein disulfide isomerase) and human Ero1α (ER oxidoreductin-1 to reoxidize PDI).
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Reagent Qty Description Storage GSSG 12.5 ul Oxidized glutathione (60 mM) -20 C PDI 25 ul Human protein disulfide isomerase with no tags (200 µM) -80 C Ero1a 25 ul Human ER oxidoreductin-1 to reoxidize PDI with no tags (5 µM) -80 C Dilution Buffer 500 ul 30% glycerol buffer -20 C
