Protein sulfenic acid formation is a reversible post-translational modification that may be used to monitor protein oxidation on reactive cysteines within target proteins. This can be detected with protein sulfenic acid derivatised with dimedone.
Specificity
This antibody recognizes proteins containing cysteine sulfenic acid derivitized with dimedone.
Immunogen
Epitope: Other
KLH-conjugated corresponding to cysteine sulfenic acid.
Application
Anti-Cysteine Sulfenic Acid detects levels of Cysteine Sulfenic Acid proteins & has been published & validated for use in WB.
Research Category Apoptosis & Cancer
Research Sub Category General Post-translation Modification
Western Blot Analysis: A previous lot of this antibody detected cysteine sulfenic acid in NIH/3T3 and HEK293 cell lysates.
Quality
Evaluated by Western Blot in rat ventricular myocyte lysate.
Western Blot Analysis: 1:10,000 dilution of this antibody detected cysteine sulfenic acid on 10 µg of rat ventricular myocyte lysate.
Target description
Multiple kDa are observed that increases with oxidized stress (H2O2).
Physical form
Unpurified
Unpurified rabbit polyclonal with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Analysis Note
Control Rat ventricular myocyte lysate
Disclaimer
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Certificates of Analysis (COA)
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The Biochemical journal, 478(7), 1453-1470 (2021-03-23)
Redox regulation of proteins via cysteine residue oxidation is involved in the control of various cellular signal pathways. Pyruvate kinase M2 (PKM2), a rate-limiting enzyme in glycolysis, is critical for the metabolic shift from glycolysis to the pentose phosphate pathway
Protein sulfenic acids (SOHs) are the principal oxidation products formed when redox active proteins interact with peroxide molecules. We have developed a new antibody reagent that detects protein SOHs derivatized with dimedone. Using this new antibody, we found that glyceraldehyde
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