Peroxiredoxin SO2/3 peptide

  • Description

  • Application Data

Description

Antigenic peptide corresponding to region of mammalian overoxidised 2-Cys peroxiredoxin 1-4 (Prx1-4)

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Application Data

Catalogue number crb1200280
Antibody Peroxiredoxin SO2/3 peptide
Antigen Peptide Peroxiredoxin SO2/3 peptide
Protein ID UniProtKB - Q13162 Human, Q06830, P32119, P30048
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
Target Protein Species Human
Storage Stabilisers -20°C
Family Peroxiredoxin family
Specificity PTM - oxidised form
Post-translational Modification Overoxidized form of Peroxiredoxin 1-4
Storage -20°C
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

References

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

Data Sheet Material Safety Data Sheet (MSDS)

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.

Peroxiredoxin SO2/3 peptide

Cat No.Pack SizePriceQty.
100µg£85.00
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