|Tested species reactivity||Human, Mouse|
|Published species reactivity||Human, Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Sulfonylated peptide, KLH coupled, corresponding to the active site sequence common to human Prx I to IV.|
|Purification||Ammonium sulfate precipitation|
|Storage buffer||HEPES with 0.15M NaCl, 0.01% BSA, 50% glycerol|
|Contains||0.03% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000-1:2000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 4 publications below|
A suggested positive control for this product is HeLa cells treated with H2O2.
Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at their active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Prx I to IV have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Prx I. The active site cysteine (Cys51) is oxidized to cysteine sulfenic acid (Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress condition, the sulfenic intermediate (Cys51-SOH) can be easily overoxidized to cysteine sulfinic acid (Cys-SO2H) or cysteine sulfonic acid (Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that overoxidized Prx can be reduced back to the active form during recovery after oxidative stress. Anti-Prx-SO3 antibody recognizes both sulfinic and sulfonic forms of Prx and detects overoxidized Prx enzymes in H2O2-treated cells with high sensitivity and specificity.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Thioredoxin-1/peroxiredoxin-1 as sensors of oxidative stress mediated by NADPH oxidase activity in atherosclerosis.
LF-PA0004 was used in western blot to investigate the role of thioredoxin-1/peroxiredoxin-1 in atherosclerosis
|Madrigal-Matute J,Fernandez-Garcia CE,Blanco-Colio LM,Burillo E,Fortuño A,Martinez-Pinna R,Llamas-Granda P,Beloqui O,Egido J,Zalba G,Martin-Ventura JL||Free radical biology and medicine (86:352)||2015|
Peroxiredoxin-2 expression is increased in beta-thalassemic mouse red cells but is displaced from the membrane as a marker of oxidative stress.
LF-PA0004 was used in western blot to investigate the expression of Prx2 in beta-thalassemic mouse red cells
|Matte A,Low PS,Turrini F,Bertoldi M,Campanella ME,Spano D,Pantaleo A,Siciliano A,De Franceschi L||Free radical biology and medicine (49:457)||2010|
Identification of cardiac myosin-binding protein C as a candidate biomarker of myocardial infarction by proteomics analysis.
LF-PA0004 was used in western blot to characterize biomarkers of acute myocardial infarction
|Jacquet S,Yin X,Sicard P,Clark J,Kanaganayagam GS,Mayr M,Marber MS||Molecular and cellular proteomics : MCP (8:2687)||2009|
Oxidation of 2-Cys-peroxiredoxins by arachidonic acid peroxide metabolites of lipoxygenases and cyclooxygenase-2.
LF-PA0004 was used in western blot to investigate the oxidation of 2-cys-peroxiredoxins mediated by lipid hydroperoxide metabolites of arachidonic acid
|Cordray P,Doyle K,Edes K,Moos PJ,Fitzpatrick FA||The Journal of biological chemistry (282:32623)||2007|