Anticorps PRX (E-7): sc-271020

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 (E-7) Références:

1. Progrès dans notre compréhension de la peroxiredoxine, une protéine redox multifonctionnelle des mammifères.  |  Fujii, J. and Ikeda, Y. 2002. Redox Rep. 7: 123-30. PMID: 12189041
2. La peroxiredoxine: un acteur central de la modulation immunitaire.  |  Robinson, MW., et al. 2010. Parasite Immunol. 32: 305-13. PMID: 20500659
3. L'adénanthine cible la peroxiredoxine I/II pour tuer les cellules de carcinome hépatocellulaire.  |  Hou, JK., et al. 2014. Cell Death Dis. 5: e1400. PMID: 25188510
4. Les rôles de la peroxirédoxine et de la thiorédoxine dans la détection du peroxyde d'hydrogène et dans la transduction du signal.  |  Netto, LE. and Antunes, F. 2016. Mol Cells. 39: 65-71. PMID: 26813662
5. Catalyse de la peroxiredoxine à résolution atomique.  |  Perkins, A., et al. 2016. Structure. 24: 1668-1678. PMID: 27594682
6. La glutathionylation de la Prx 2-Cys du chloroplaste de pois et de la Prx IIF mitochondriale affecte leur structure et leur activité peroxydase, et la sulfiredoxine déglutathionyle uniquement la Prx 2-Cys.  |  Calderón, A., et al. 2017. Front Plant Sci. 8: 118. PMID: 28197170
7. Détection de la lumière par le peroxyde d'hydrogène et une peroxiredoxine.  |  Bodvard, K., et al. 2017. Nat Commun. 8: 14791. PMID: 28337980
8. Reconstruction de l'assemblage de type anneau de la peroxirédoxine par modification chimique.  |  Himiyama, T., et al. 2021. Bioconjug Chem. 32: 153-160. PMID: 33334100
9. Les écarts par rapport à la pression artérielle optimale dérivée de la PRx sont associés à la mortalité après un arrêt cardiaque.  |  Kirschen, MP., et al. 2022. Resuscitation. 175: 81-87. PMID: 35276311

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