Anticorps PRX (G-10): sc-137212

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 (G-10) Références:

1. La mutagenèse et la modélisation du complexe peroxiredoxine (Prx) avec la structure RMN de la sulfiredoxine humaine liée à l'ATP impliquent l'aspartate 187 de Prx I comme résidu catalytique dans l'hydrolyse de l'ATP.  |  Lee, DY., et al. 2006. Biochemistry. 45: 15301-9. PMID: 17176052
2. Systèmes de peroxiredoxine chez les mycobactéries.  |  Jaeger, T. 2007. Subcell Biochem. 44: 207-17. PMID: 18084895
3. La peroxiredoxine fonctionne comme une peroxydase et comme un régulateur et un capteur de peroxydes locaux.  |  Rhee, SG., et al. 2012. J Biol Chem. 287: 4403-10. PMID: 22147704
4. L'enzyme antioxydante peroxiredoxine et son rôle protecteur dans les troubles neurologiques.  |  Zhu, H., et al. 2012. Exp Biol Med (Maywood). 237: 143-9. PMID: 22302711
5. Rôle de la sulfiredoxine en tant que régulateur de la fonction de la peroxiredoxine et régulation de son expression.  |  Jeong, W., et al. 2012. Free Radic Biol Med. 53: 447-56. PMID: 22634055
6. Rôle de la famille des peroxirédoxines dans la signalisation du cancer.  |  Kim, Y. and Jang, HH. 2019. J Cancer Prev. 24: 65-71. PMID: 31360686
7. Peroxiredoxin (2-cys-prx) et catalase (katA): des bioreporters bioluminescents à base de cyanobactéries pour détecter le stress oxydatif dans l'environnement aquatique.  |  Hurtado-Gallego, J., et al. 2019. Chemosphere. 236: 124395. PMID: 31545198
8. Diminution de l'expression de la peroxiredoxine chez les patientes atteintes de kystes d'endométriose ovarienne.  |  Yu, H., et al. 2020. Arch Med Res. 51: 670-674. PMID: 32564961
9. Activité et fonction de la peroxiredoxine-IIF (PRXIIF) mitochondriale au cours du vieillissement des graines.  |  Klupczyńska, EA., et al. 2022. Antioxidants (Basel). 11: PMID: 35883717
10. Protocole fluorométrique pour l'estimation de l'activité de la peroxiredoxine dans les tissus biologiques.  |  Hussein, MJ. and Hadwan, MH. 2023. J Fluoresc. 33: 721-730. PMID: 36508000

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