|Tested species reactivity||Human|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Sulfonylated peptide, KLH coupled, corresponding to the active site sequence common to mammalian Prx I to IV.|
|Storage buffer||HEPES with 0.15M NaCl, 0.01% BSA, 50% glycerol|
|Contains||0.03% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||0.5 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
A suggested positive control for this product is HeLa cells treated with H2O2.
Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at their active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Prx I to IV have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Prx I. The active site cysteine (Cys51) is oxidized to cysteine sulfenic acid (Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress condition, the sulfenic intermediate (Cys51-SOH) can be easily overoxidized to cysteine sulfinic acid (Cys-SO2H) or cysteine sulfonic acid (Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that overoxidized Prx can be reduced back to the active form during recovery after oxidative stress. Anti-Prx-SO3 antibody recognizes both sulfinic and sulfonic forms of Prx and detects overoxidized Prx enzymes in H2O2-treated cells with high sensitivity and specificity.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.