|Detection of Human/Mouse Peroxiredoxin 5 by Western Blot. Western blot shows lysates of MCF-7 human breast cancer cell line, HepG2 human hepatocellular carcinoma cell line, K562 human chronic myelogenous leukemia cell line, A431 human epithelial carcinoma cell line, and NIH-3T3 mouse embryonic fibroblast cell line. PVDF membrane was probed with 0.5 µg/mL of Human/Mouse Peroxiredoxin 5 Antigen Affinity‑purified Polyclonal Antibody (Catalog # AF3774) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Peroxiredoxin 5 at approximately 17 kDa (as indicated). This experiment was conducted using Immunoblot Buffer Group 2.|
Peroxiredoxin-5 (Prx-5 or PRDX5; also AOEB166 and thioredoxin reductase) is a 22 kDa, widely expressed mitochondrial antioxidant enzyme that belongs to the atypical 2-Cys class of the TSA/ahpC family of peroxiredoxins. The precursor molecule is 214 amino acids (aa) in length. It contains an N-terminal 52 aa mitochondrial targeting (signal) sequence and a 162 aa (17 kDa) mature enzyme that shows a nuclear export signal between aa 58‑67, and a peroxisome targeting motif at aa 212‑214. There are two catalytic cysteines, one at Cys100 and a second at Cys204 of the precursor. Prx-5 is a monomer that is found in mitochondria, cytosol, nucleus and peroxisomes. It is known to reduce H2O2 and alkyl hydroperoxides. Prx5 can undergo cleavage after Ala52, generating two splice forms. One shows a deletion of aa 59‑147, while a second shows a deletion of aa 103‑146. Mature human Prx-5 is 78% aa identical to mouse Prx-5, with most differences noted over the first 52 amino acids.
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