PRX Antibody (C-6): sc-271047

PRX Antibody (C-6) is a mouse monoclonal IgG2b antibody that detects peroxiredoxin (PRX) in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-PRX antibody (C-6) targets a crucial family of antioxidant proteins that play a significant role in cellular defense against reactive oxygen species (ROS), which can cause oxidative stress and damage to cellular components. PRX (C-6) monoclonal antibody recognizes peroxiredoxin proteins, including PRX I, II, III, IV, V, and VI, primarily localized in the cytoplasm and mitochondria, where these proteins utilize thioredoxin as an electron donor to reduce hydroperoxides, thereby preventing oxidative damage. This localization allows PRX proteins to effectively neutralize ROS in key cellular compartments, contributing to cell proliferation, differentiation, and gene expression regulation. PRX I, II, and III have been implicated in the pathogenesis of various diseases, including breast cancer and neurodegenerative disorders such as Alzheimer′s disease, highlighting their importance in both normal physiology and disease states. The human PRX I gene is expressed in multiple tissues, including the liver, kidney, testis, lung, and nervous system, while PRX II is predominantly found in the testis, and PRX III is expressed in the lung. The diverse expression patterns and functional roles of these proteins underscore their significance in maintaining cellular homeostasis and responding to oxidative stress, making anti-PRX antibody (C-6) an essential tool for researchers studying oxidative stress and related pathologies.

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PRX Antibody (C-6) References:

1. 2-Cys peroxiredoxin function in intracellular signal transduction: therapeutic implications.  |  Kang, SW., et al. 2005. Trends Mol Med. 11: 571-8. PMID: 16290020
2. Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling.  |  Cox, AG., et al. 2009. Biochem J. 425: 313-25. PMID: 20025614
3. Effect of PRX-1 Downregulation in the Type 1 Diabetes Microenvironment.  |  Yoo, JS., et al. 2012. Korean J Physiol Pharmacol. 16: 463-8. PMID: 23269909
4. Nicotinamide nucleotide transhydrogenase (Nnt) links the substrate requirement in brain mitochondria for hydrogen peroxide removal to the thioredoxin/peroxiredoxin (Trx/Prx) system.  |  Lopert, P. and Patel, M. 2014. J Biol Chem. 289: 15611-20. PMID: 24722990
5. Peroxiredoxin post-translational modifications by redox messengers.  |  Riquier, S., et al. 2014. Redox Biol. 2: 777-85. PMID: 25009779
6. Site-directed mutagenesis substituting cysteine for serine in 2-Cys peroxiredoxin (2-Cys Prx A) of Arabidopsis thaliana effectively improves its peroxidase and chaperone functions.  |  Lee, EM., et al. 2015. Ann Bot. 116: 713-25. PMID: 26141131
7. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.  |  Nelson, KJ., et al. 2018. Antioxid Redox Signal. 28: 521-536. PMID: 28375740
8. Regulation of cartilage damage caused by lack of Klotho with thioredoxin/peroxiredoxin (Trx/Prx) system and succedent NLRP3 activation in osteoarthritis mice.  |  Gu, Y., et al. 2019. Am J Transl Res. 11: 7338-7350. PMID: 31934282
9. Hierarchical peroxiredoxin assembly through orthogonal pH-response and electrostatic interactions.  |  Anaya-Plaza, E., et al. 2023. J Mater Chem B. 11: 11544-11551. PMID: 37990925
10. A New Fluorescent Method for Measuring Peroxiredoxin Enzyme Activity Using Monobromobimane.  |  Mohsin, NY., et al. 2024. J Fluoresc.. PMID: 39441257

The preferred PRX antibody is PRX Antibody (B-11): sc-137222.