DsbC Set

GFK

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 µ M *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).
-
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 µ M)
-80 C
Ero1a
25 ul
Human ER oxidoreductin-1 to reoxidize PDI with no tags (5 µ M)
-80 C
Dilution Buffer
500 ul
30% glycerol buffer
-20 C