Anti-Peroxiredoxin SO2/3 antibody


Recognises mammalian overoxidised 2-Cys peroxiredoxin 1-4 (Prx1-4) with a strong signal and low background noise

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Application Data

Catalogue number crb2005004
Antibody Anti-Peroxiredoxin SO2/3 Antibody
Antigen Peptide KLH conjugated synthetic peptide crb1200280e
Protein ID UniProtKB - Q06830,P32119, P30048, Q13162
Aliases PRDX3, Thioredoxin-dependent peroxide reductase, mitochondrial/ Antioxidant protein 1, AOP-1, HBC189, PRDX2, PRX III, Peroxiredoxin, PRP, PRX II, Natural Killer cell-enhancing factor B, NKEF-B, Thiol-specific antioxidant protein, TSA
Cross-Reactivity Human, frog
Host Species Anti-Rabbit
Antibody Type Polyclonal
Label Unconjugated
Concentration 1mg/ml
Validation WB/ELISA
Target Peroxiredoxin SO2/3
Disease Area Cancer, Circadian Rhythm
Family Peroxiredoxin family
Specificity PTM - oxidised form
Post-translational Modification Overoxidized form of Peroxiredoxin 1-4
Storage This material is supplied in PBS containing 0.01% sodium azide and 1% trehalose. The product should be stored at +4°C for short term storage and -20°C for long term storage. Avoid repeated freeze/ thaw cycles.
Citations Milev, N., Rey, G., Valekunja, U., Edgar, R., O’Neill, J. and Reddy, A. (2015). Analysis of the Redox Oscillations in the Circadian Clockwork. Methods Enzymol, 185-210. PMID: 25707278

Ishida, Y., Takikawa, M., Suzuki, T., Nagahama, M. and Ogasawara, Y. (2014). Irreversible hyperoxidation of peroxiredoxin 2 is caused by tert-butyl hydroperoxide in human red blood cells. FEBS Open Bio, 4(1), 848-852. PMID: 25379381


Park, S-J., Kim, T-S., Kim, J-M., Chang, K-T., Lee, H-S. and Lee, D-S. (2015). Repeated Superovulation via PMSG/hCG Administration Induces 2-Cys Peroxiredoxins Expression and Overoxidation in the Reproductive Tracts of Female Mice. Mol Cells, 38(12), 1071-1078. PMID: 26486164

Peroxiredoxins (Prxs) are a recently identified highly abundant and reactive family of antioxidant enzymes that reduce H2O2 via cysteine residue reactivity and make up the major cellular sink for cellular peroxides. Prxs are essential for preventing neurodegenerative disorders, haemolytic anaemia and inflammation from oxidative stress through the elimination of H2O2.

The cysteine residues of Prx1-4 proteins are converted to thioredoxin (Trx) via a sulfenic intermediate and a disulphide bridge. However due to the slow rate of conversion to the disulfide, the sulfenic intermediate is occasionally over-oxidized to cysteine sulfinic acid (Cys-SO2H) or cysteine sulfonic acid (Cys-SO3H), which leads to the inactivation of the peroxidase activity. Prx proteins exhibit circadian cycles in their oxidation status in the absence of transcription and the inactivated form of the enzyme displays circadian accumulation.

Overoxidized Prxs are also seen in excessive oxidative stress conditions such as the balloon-injured rat carotids, human atherosclerotic lesions, Pyrazole-induced liver Injury, and aged rat liver.

Anti-Peroxiredoxin SO2/3 antibody

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