anti-Peroxiredoxin 6-SO3, pAb

Peroxiredoxin VI (Prx 6, 1-Cys Prx) is a member of Peroxiredoxin Family, an antioxidant enzyme that detoxifies reactive oxygen species and has a cysteine at their active site. Six isoforms (Prx 1 to 6) of Prx exist in all eukaryotic cells. These isoforms are classified into three subgroups (2-Cys, atypical 2-Cys, and 1-Cys). Prx 6 modulates various receptor-signaling pathways and protects cells from cell death induced by oxidative stress. The active site cysteine (Cys47) is oxidized to cysteine sulfenic acid (Cys47-SOH) by H2O2. However, the resulting Cys47-SOH does not form a disulfide bond because of unavailability of another Cys-SH nearby. It can be reduced by nonphysiological thiols such as DDT but is not transformed by Thioredoxin/Thioredoxin Reductase or GSH. Occasionally, the sulfenic intermediate is hyperoxidized to sulfinic or sulfonic acid, resulting in inactivation of peroxidase activity. Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.