|Detection of Human and Mouse Peroxiredoxin 3 by Western Blot. Western blot shows lysates of TF‑1 human erythroleukemic cell line and mouse spleen tissue. PVDF Membrane was probed with 1 µg/mL of Human/Mouse Peroxiredoxin 3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6610) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Peroxiredoxin 3 at approximately 28 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
Peroxiredoxin-3 (Prx-3/III; also AOP-1, MER5 and thioredoxin-dependent peroxidase reductase) is a ubiquitous, 22-28 kDa mitochondrial antioxidant enzyme that belongs to the 2-Cys class of the TSA/ahpC family of peroxiredoxins. Prx-3 is known to act as either a homodimer, or a decamer, and scavenge reactive oxygen species generated by oxidative stress. The mouse Prx-3 precursor molecule is 257 amino acids (aa) in length. It contains a cleavable N-terminal 63 aa mitochondrial targeting sequence, plus a 194 aa mature enzyme that shows a thioredoxin domain between aa 64-222. There are two catalytic cysteines, one at Cys109 and another at Cys230 of the precursor. Prx-3 undergoes a phosphorylation at Thr147 that reduces its activity. One potential splice form shows a deletion of Arg149, Lys150 and Arg185. Full-length mouse Prx-3 is 86% and 95% aa identical to human and rat Prx-3, respectively.
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