immunoprecipitation (IP): 2.0-5.0 μg using lysate of mouse 3T3 cells western blot: 0.5-1.0 using whole extract of human HeLa cells western blot: 1-2 μg/mL using whole extract of rat NRK cells
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immunoprecipitation (IP): 2.0-5.0 μg using lysate of mouse 3T3 cells western blot: 0.5-1.0 using whole extract of human HeLa cells western blot: 1-2 μg/mL using whole extract of rat NRK cells
Peroxiredoxin 2 is a cytosolic member of the peroxiredoxin family of antioxidant enzymes. All peroxiredoxin enzymes exist as homodimers, they contain a conserved Cys residue corresponding to Cys51 in mammalian peroxiredoxin 1 and 2 and are distributed differentially within cells.
Immunogen
synthetic peptide corresponding to amino acid residues 184-198 of human peroxiredoxin 2 conjugated to KLH. The corresponding sequence is identical in rat and mouse peroxiredoxin 2.
Application
Anti-Peroxiredoxin 2 (C-terminal) antibody produced in rabbit has been used in immunoblottingand immunoprecipitation.[1]
Biochem/physiol Actions
Peroxiredoxin 2 has dual roles as a peroxireductase in moderately oxidative conditions and as a molecular chaperone that binds and protects denatured proteins in hyper-oxidative conditions. Peroxiredoxin 2 is involved in platelet-derived growth factor (PDGF) and tumor necrosis factor (TNF) signaling regulation and is elevated in several human cancers and neurodegenerative disorders.
Physical form
Solution in 0.01 M phophate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death
Moon JC, et al.
Test, 280(31), 28775-28784 (2005)
Loss of peroxiredoxin-2 exacerbates eccentric contraction-induced force loss in dystrophin-deficient muscle
Olthoff JT, et al.
Nature Communications, 9(1), 5104-5104 (2018)
Glutathionylation of the active site cysteines of peroxiredoxin 2 and recycling by glutaredoxin
Peskin AV, et al.
The Journal of Biological Chemistry, 291(6), 3053-3062 (2016)
The Journal of biological chemistry, 292(35), 14371-14380 (2017-07-08)
Regulation of growth factor signaling involves reversible inactivation of protein tyrosine phosphatases (PTPs) through the oxidation and reduction of their active site cysteine. However, there is limited mechanistic understanding of these redox events and their co-ordination in the presence of
The Journal of biological chemistry, 291(6), 3053-3062 (2015-11-26)
Peroxiredoxin 2 (Prx2) is a thiol protein that functions as an antioxidant, regulator of cellular peroxide concentrations, and sensor of redox signals. Its redox cycle is widely accepted to involve oxidation by a peroxide and reduction by thioredoxin/thioredoxin reductase. Interactions
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