|Tested species reactivity||Human|
|Published species reactivity||Mouse, Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Sulfonylated peptide (KLH coupled) corresponding to the active site sequence common to mammalian Prx 6.|
|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)||1:2000|
* 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 2 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.
|Not Applicable||Not Cited||
Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity.
LF-PA0005 was used in western blot to determine the requirement of glutathione S-transferase pi and peroxiredoxin 6 homodimerization for peroxidase and not phospholipase A2 activity
|Zhou S,Sorokina EM,Harper S,Li H,Ralat L,Dodia C,Speicher DW,Feinstein SI,Fisher AB||Free radical biology and medicine (94:145)||2016|
Identification of cardiac myosin-binding protein C as a candidate biomarker of myocardial infarction by proteomics analysis.
LF-PA0005 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|