Anticorps PRX (H-6): sc-373961

The peroxiredoxin (PRX) family comprises six antioxidant proteins, PRX I, II, III, IV, V and VI, which protect cells from reactive oxygen species (ROS) by preventing the metal-catalyzed oxidation of enzymes. The PRX proteins primarily utilize thioredoxin as the electron donor for antioxidation, although they are fairly promiscuous with regard to the hydroperoxide substrate. In addition to protection from ROS, peroxiredoxins are also involved in cell proliferation, differentiation and gene expression. PRX I, II, IV and VI show diffuse cytoplasmic localization, while PRX III and V exhibit distinct mitochondrial localization. The human PRX I gene encodes a protein that is expressed in several tissues, including liver, kidney, testis, lung and nervous system. PRX II is expressed in testis, while PRX III shows expression in lung. PRX I, II and III are overexpressed in breast cancer and may be involved in its development or progression. Upregulated protein levels of PRX I and II in Alzheimer's disease (AD) and Down syndrome (DS) indicate the involvement of PRX I and II in their pathogenesis. The human PRX IV gene is abundantly expressed in many tissues. PRX IV exists as a precursor protein, which is only detected in testis, and a processed secreted form. PRX V also exists as two forms, designated long and short. Like PRX IV, the long form of PRX V is highly expressed in testis. The short form of PRX V is more widely expressed, with high expression in liver, kidney, heart and lung. PRX VI, a 1-Cys peroxiredoxin (also known as antioxidant protein 2 or AOP2), is highly expressed in most tissues, particularly in epithelial cells. Localized to the cell cytosol, PRX VI functions independently of other peroxiredoxins and antioxidant proteins, specializing in antioxidant defense, lung phospholipid metabolism and protection of keratinocytes from cell death induced by reactive oxygen species.

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Anticorps PRX (H-6) Références:

1. Peroxiredoxine dépendante de la glutaredoxine du peuplier: interaction protéine-protéine et mécanisme catalytique.  |  Rouhier, N., et al. 2002. J Biol Chem. 277: 13609-14. PMID: 11832487
2. Régulation à la baisse de la peroxiredoxine spécifique de l'isoforme dans le myocarde humain défaillant.  |  Brixius, K., et al. 2007. Life Sci. 81: 823-31. PMID: 17727896
3. Rôle anti-apoptotique de la peroxiredoxine III dans les cellules cancéreuses du col de l'utérus.  |  Li, L., et al. 2013. FEBS Open Bio. 3: 51-4. PMID: 23772374
4. Évaluation de la sensibilité de la peroxiredoxine à l'inactivation par des substrats de peroxyde.  |  Nelson, KJ., et al. 2013. Methods Enzymol. 527: 21-40. PMID: 23830624
5. La déficience en SOD1 induit une hyperoxydation systémique de la peroxiredoxine chez la souris.  |  Homma, T., et al. 2015. Biochem Biophys Res Commun. 463: 1040-6. PMID: 26079888
6. Limite inférieure de la réactivité évaluée avec PRx dans un cadre expérimental.  |  Beqiri, E., et al. 2021. Acta Neurochir Suppl. 131: 275-278. PMID: 33839857
7. Protocole exact et précis pour estimer l'activité de l'enzyme peroxiredoxine.  |  Hamza, T. and Hadwan, MH. 2021. Rep Biochem Mol Biol. 10: 156-163. PMID: 34604405
8. Les fluctuations à l'état natif dans un site actif de la peroxiredoxine correspondent aux mouvements nécessaires à la catalyse.  |  Estelle, AB., et al. 2022. Structure. 30: 278-288.e3. PMID: 34678159
9. La peroxiredoxine mitochondriale de Trypanosoma cruzi favorise l'infectivité dans les macrophages et atténue la toxicité du nifurtimox.  |  Specker, G., et al. 2022. Front Cell Infect Microbiol. 12: 749476. PMID: 35186785
10. Le cisplatine induit des lésions rénales par le biais de la régulation à la baisse de la Prx I par dégradation autophagique.  |  Park, J., et al. 2024. Free Radic Biol Med. 225: 236-246. PMID: 39366472

L'anticorps PRX préféré est l'Anticorps PRX (B-11): sc-137222.