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Cysteine (sulfonate) polyclonal antibody

ADI-OSA-820-D 50 µg Inquire for pricing
ADI-OSA-820-F 200 µg Inquire for pricing
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This antibody detects sulfenic, sulfonic and sulfinic acid modified proteins.

Product Details

Immunogen:Recombinant human cysteine (sulfonate). Cysteamine backbone modified by dimedone with a five-carbon linker to KLH.
Source:Purified from rabbit serum.
Species reactivity:Human
Specificity:Recognizes all forms of cysteine with an oxidized thiol group (sulfenic RSOH, sulfinic RSO2H and sulfonic RSO3H).
Recommended Dilutions/Conditions:Western Blot (1:1,000, ECL)
Detection of sulfenic, sulfonic, and sulfinic acid-modified proteins by Western Blot requires the pre-treatment of cells with dimedone as described in Seo and Carroll (2009).
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Purity Detail:Protein A affinity purified.
Formulation:Liquid. In PBS containing 50% glycerol and 0.09% sodium azide.
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
Scientific Background: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.
Regulatory Status:RUO - Research Use Only

Product Literature References

Cholesterol crystals increase vascular permeability by inactivating SHP2 and disrupting adherens junctions: A.M. Mani, et al.; Free Radic. Biol. Med. 123, 72 (2018), Application(s): Western blot, Abstract;
Resolvin D1 via prevention of ROS-mediated SHP2 inactivation protects endothelial adherens junction integrity and barrier function: R. Chattopadhyay, et al.; Redox Biol. 12, 438 (2017), Application(s): Western blot, Abstract; Full Text

General Literature References

Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies: Y.H. Seo & K.S. Carroll; PNAS 106, 16163 (2009), 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;

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