Peroxiredoxin-6 (human, recombinant)

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.

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1. Arevalo, J.A., and Vázquez-Medina, J.P. The role of peroxiredoxin 6 in cell signaling. Antioxidants (Basel) 7(12), 172 (2018).

2. Choi, H.J., Kang, S.W., Yang, C.H., et al. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat. Struct. Biol. 5(5), 400-406 (1998).

3. Dammeyer, P., and Arnér, E.S. Human Protein Atlas of redox systems - What can be learnt? Biochim. Biophys. Acta 1810(1), 111-138 (2011).

4. Chen, J.W., Dodia, C., Feinstein, S.I., et al. 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A₂ activities. The Journal of Biological Chemisty 275(37), 28421-28427 (2000).

5. Fisher, A.B., Dodia, C., Sorokina, E.M., et al. A novel lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6. J. Lipid Res. 57(4), 587-596 (2016).

6. Jia, W., Dong, C., and Li, B. Anti-oxidant and pro-oxidant effects of peroxiredoxin 6: A potential target in respiratory diseases. Cells 12(1), 181 (2023).