PRX Antibody (G-10): sc-137212

PRX Antibody (G-10) is a mouse monoclonal IgG1 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 (G-10) 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 by preventing oxidative damage, which can lead to various diseases, including cancer and neurodegenerative disorders. Notably, PRX I, II, and III have been implicated in breast cancer, as their overexpression may contribute 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 specifically localized to mitochondria, underscoring their distinct roles in cellular metabolism and antioxidant defense. The human PRX IV gene, which is abundantly expressed across various tissues, produces both a precursor protein and a processed secreted form, further illustrating the complexity and functional diversity of the peroxiredoxin family. PRX monoclonal antibody (G-10) is an invaluable tool for researchers studying oxidative stress and its 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 (G-10) References:

1. Mutagenesis and modeling of the peroxiredoxin (Prx) complex with the NMR structure of ATP-bound human sulfiredoxin implicate aspartate 187 of Prx I as the catalytic residue in ATP hydrolysis.  |  Lee, DY., et al. 2006. Biochemistry. 45: 15301-9. PMID: 17176052
2. Peroxiredoxin systems in mycobacteria.  |  Jaeger, T. 2007. Subcell Biochem. 44: 207-17. PMID: 18084895
3. Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides.  |  Rhee, SG., et al. 2012. J Biol Chem. 287: 4403-10. PMID: 22147704
4. The antioxidant enzyme peroxiredoxin and its protective role in neurological disorders.  |  Zhu, H., et al. 2012. Exp Biol Med (Maywood). 237: 143-9. PMID: 22302711
5. Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression.  |  Jeong, W., et al. 2012. Free Radic Biol Med. 53: 447-56. PMID: 22634055
6. The Role of Peroxiredoxin Family in Cancer Signaling.  |  Kim, Y. and Jang, HH. 2019. J Cancer Prev. 24: 65-71. PMID: 31360686
7. Peroxiredoxin (2-cys-prx) and catalase (katA) cyanobacterial-based bioluminescent bioreporters to detect oxidative stress in the aquatic environment.  |  Hurtado-Gallego, J., et al. 2019. Chemosphere. 236: 124395. PMID: 31545198
8. Decreased Expression of Peroxiredoxin in Patients with Ovarian Endometriosis Cysts.  |  Yu, H., et al. 2020. Arch Med Res. 51: 670-674. PMID: 32564961
9. Mitochondrial Peroxiredoxin-IIF (PRXIIF) Activity and Function during Seed Aging.  |  Klupczyńska, EA., et al. 2022. Antioxidants (Basel). 11: PMID: 35883717
10. Fluorometric Protocol for Estimating Peroxiredoxin Activity in Biological Tissues.  |  Hussein, MJ. and Hadwan, MH. 2023. J Fluoresc. 33: 721-730. PMID: 36508000

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