Anti-Cysteine (sulfonate) Antibody (OAED00119)

Catalog No: OAED00119

Size:50 ug

Western blot analysis of Cysteine (sulfonate), pAb: Lane 1:MW marker Lane 2: HeLa Cell Lysate; Lane 3: HeLa Cell Lysate, Heat Shocked.

Product Info

• Predicted Species Reactivity: Human
• Product Format: Liquid. PBS containing 50% glycerol and 0.09% sodium azide.
• Clonality: Polyclonal
• Host: Rabbit
• Application: WB
• Reconstitution and Storage: Store at -20°C
• Immunogen: Recombinant human cysteine (sulfonate). Cysteamine backbone modified by dimedone with a five-carbon linker to KLH.
• Purification: Protein A affinity purified.
• Concentration: 1 mg/ml
• Specificity: Recognizes all forms of cysteine with an oxidized thiol group (sulfenic RSOH, sulfinic RSO2H and sulfonic RSO3H).
• Intended Use: For research use only.
• Application Info: WB: 1:1000 ECL
  Detection of sulfenic, sulfonic, and sulfinic acid-modified proteins by Western Blot requires the pre-treatment of cells with dimedone.
  Optimal dilutions should be determined by the end user.
• Reference: Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies: Y.H. Seo & K.S. Carroll; PNAS 106, 16163 (2009), Application(s): Immunofluorescence and western-blotting using HeLa cells, Abstract; Full Text
  A chemical approach for detecting sulfenic acid-modified proteins in living cells: K.G. Reddie, et al.; Mol. Biosyst. 4, 521 (2008), Abstract;
  Expanding the functional diversity of proteins through cysteine oxidation: K.G. Reddie & K.S. Carroll; Curr. Opin. Chem. Biol. 12, 746 (2008), Abstract;
  Protein sulfenic acids in redox signaling: L.B. Poole, et al.; Annu. Rev. Pharmacol. Toxicol. 44, 325 (2004), Abstract;
• Publications:

  Pimozide Alleviates Hyperglycemia in Diet-Induced Obesity by Inhibiting Skeletal Muscle Ketone Oxidation. Cell Metab. 31, 909-919.e8 (2020) 32275862

Target Info

• Gene Symbol: Cysteine
• Description of Target: Reduction and oxidation (redox) play a critical role in a wide variety of biological processes including respiration, photosynthesis, proteostasis, and cell stress, among others. Redox signaling is accomplished by networks of regulatory enzymes and proteins which modulate the oxidative state of biological molecules, with cysteine thiol side chains playing a critical role. The highly nucleophilic and polarizable sulfur atom can occupy sulfenic (RSOH), sulfinic (RSO2H) or sulfonic (RSO3H) states. Within a protein body, the various redox forms of cysteine can be transiently stabilized and play an active role in regulating or altering protein activity or absorbing oxidative stress. The ability to stabilize and quantify these oxidative forms allows analysis of redox regulation at a level of detail which transcends traditional methods that quantify protein or free radicals. Chemical modification can be utilized to stabilize these transient oxidative forms for subsequent detection, and has been successfully employed in the detection of the sulfenic acid form.