Peroxiredoxin-2 (human, recombinant)

Peroxiredoxin-2 (Prx2) is a typical 2-Cys-containing Prx that is involved in the maintenance of cellular thiol redox homeostasis. It exists as a homodimer and is composed of a thioredoxin fold-containing catalytic domain, which contains peroxidatic and resolving cysteines (Cp and Cr, respectively), and a C-terminal arm. Prx2 is ubiquitously expressed and localizes to the cytosol, nucleus, mitochondria, and peroxisomes. During the catalytic cycle, hydrogen peroxide oxidizes Cp to form a sulfenic acid intermediate (C-SOH), which reacts with the Cr of the opposite subunit to form a disulfide bond that is subsequently restored to a reduced state by thioredoxin (Trx) or other thiols. Prx2 primarily acts on hydrogen peroxide but also reduces other peroxides, including lipid hydroperoxides, protein peroxides, peroxynitrite, and peroxymonocarbonate and plays an important role in resolution of oxidized hemoglobin and erythrocyte membranes. Cerebrospinal fluid levels of Prx2 are increased in patients with subarachnoid hemorrhage, and substantia nigra levels of Prx2 are increased in patients with Parkinson's disease. Prx2 acts as a tumor-suppressor or -promotor in a context-dependent manner in various cancers. Cayman's Peroxiredoxin-2 (human, recombinant) protein can be used for enzyme activity assays. This protein consists of 217 amino acids and has a calculated molecular weight of 24 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 27 kDa.. Protein function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). [The UniProt Consortium]