Peroxiredoxin-6 (Prx6) is a 1-Cys-containing Prx that is involved in the maintenance of cellular thiol redox homeostasis and phospholipid metabolism.1 It exists as a homodimer and is composed of a thioredoxin fold-containing catalytic domain, which contains a peroxidatic cysteine (Cp), and a C-terminal arm.2 Unlike 2-Cys-containing Prxs, Prx6 does not contain a resolving cysteine (Cr) and uses glutathione (GSH) instead. Prx6 is ubiquitously expressed and localizes to the cytosol, nucleus, mitochondria, and plasma membrane.1,3 It has three enzymatic activities: glutathione peroxidase (GPX), acidic calcium-independent phospholipase A2 (aiPLA2), and lysophosphatidylcholine acyltransferase (LPCAT).1,4,5 The LPCAT activity, which selectively uses palmitoyl-CoA as a substrate, is coupled to the aiPLA2 activity and is selective for lysophosphatidylcholine over lysophosphatidylethanolamine, lysophosphatidylglycerol, lysophosphatidylinositol, and lysophosphatidylserine.5 These activities, coupled with the GPX activity, provide Prx6 the ability to repair oxidized cell membranes.1 Prx6 is also involved in the activation of NADPH oxidase 2 (NOX2). Tumor levels of Prx6 are increased in patients with non-small cell lung cancer (NSCLC) and serum levels of Prx6 are decreased in patients with asthma.6 Cayman’s Peroxiredoxin-6 (human, recombinant) protein consists of 235 amino acids and has a calculated molecular weight of approximately 25 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 26.5 kDa.WARNING This product is not for human or veterinary use.
