PRX Antibody (H-6): sc-373961

PRX Antibody (H-6) is a mouse monoclonal IgG1 antibody that detects peroxiredoxin (PRX) in human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-PRX antibody (H-6) targets a crucial member of the peroxiredoxin family, which consists of six antioxidant proteins that play a vital role in cellular defense against reactive oxygen species (ROS). These proteins are essential for maintaining cellular homeostasis, as they prevent oxidative damage that can lead to various diseases, including cancer and neurodegenerative disorders. Notably, PRX I, II, and III have been implicated in breast cancer, with their overexpression potentially contributing to tumor development and progression. Additionally, PRX I and II have been associated with the pathogenesis of Alzheimer′s disease and Down syndrome, highlighting their importance in neuroprotection and cellular signaling. The localization of PRX proteins varies, with PRX I, II, IV, and VI predominantly found in the cytoplasm, while PRX III and V are localized to mitochondria, emphasizing their distinct roles in cellular metabolism and oxidative stress response. The human PRX I gene is expressed in multiple tissues, including the liver, kidney, testis, lung, and nervous system, underscoring its widespread significance in physiological processes. Anti-PRX antibody (H-6) enables researchers to gain valuable insights into the functional dynamics of peroxiredoxins and their implications in health and disease.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

PRX Antibody (H-6) References:

1. Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism.  |  Rouhier, N., et al. 2002. J Biol Chem. 277: 13609-14. PMID: 11832487
2. Isoform-specific downregulation of peroxiredoxin in human failing myocardium.  |  Brixius, K., et al. 2007. Life Sci. 81: 823-31. PMID: 17727896
3. Anti-apoptotic role of peroxiredoxin III in cervical cancer cells.  |  Li, L., et al. 2013. FEBS Open Bio. 3: 51-4. PMID: 23772374
4. Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates.  |  Nelson, KJ., et al. 2013. Methods Enzymol. 527: 21-40. PMID: 23830624
5. SOD1 deficiency induces the systemic hyperoxidation of peroxiredoxin in the mouse.  |  Homma, T., et al. 2015. Biochem Biophys Res Commun. 463: 1040-6. PMID: 26079888
6. Lower Limit of Reactivity Assessed with PRx in an Experimental Setting.  |  Beqiri, E., et al. 2021. Acta Neurochir Suppl. 131: 275-278. PMID: 33839857
7. Accurate and Precise Protocol to Estimate the Activity of Peroxiredoxin Enzyme.  |  Hamza, T. and Hadwan, MH. 2021. Rep Biochem Mol Biol. 10: 156-163. PMID: 34604405
8. Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.  |  Estelle, AB., et al. 2022. Structure. 30: 278-288.e3. PMID: 34678159
9. Trypanosoma cruzi Mitochondrial Peroxiredoxin Promotes Infectivity in Macrophages and Attenuates Nifurtimox Toxicity.  |  Specker, G., et al. 2022. Front Cell Infect Microbiol. 12: 749476. PMID: 35186785
10. Cisplatin induces kidney damage through the down-regulation of Prx I by autophagic degradation.  |  Park, J., et al. 2024. Free Radic Biol Med. 225: 236-246. PMID: 39366472

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