DYn-2 Sulfenic Acid Probe

DYn-2 is a chemoselective probe for detecting sulfenylated proteins in intact cells.


  • Consists of 1,3-cyclohexanedione coupled to an alkyne moiety
  • Cyclohexanedione group selectively reacts with protein sulfenic acid modifications
  • Alkyne group of DYn-2 can then be detected using azide-bearing tags by standard click chemistry
  • Can be used with deuterated analog DYn-2-d6 (which differs in MW by 6 Da) for quantitative analysis of cells stimulated with ROS

Mild oxidation can convert the sulfhydryl group of cysteine residues on proteins to cysteine-sulfenic acid derivatives (Cys-SOH). Protein sulfenylation is a post-translational modification that is relevant to redox signaling. DYn-2 and DYn-2-d6 differ in molecular weight by 6 Da. and can be used for quantitative analysis of cells stimulated with reactive oxygen species.

From the laboratory of Kate Carroll, PhD, The Scripps Research Institute.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
DYn-2 Sulfenic Acid Probe, 10mg
10mg Currently unavailable
Regular Price:$120.00
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DYn-2 Sulfenic Acid Probe, 25mg
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Regular Price:$240.00
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DYn-2 Sulfenic Acid Probe, 50mg
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Regular Price:$475.00
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DYn-2 Sulfenic Acid Probe, 100mg
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Product Type: Small Molecule
Name: DYn-2
Chemical Formula: C11H14O2
Molecular Weight: 178.23
Format: White Solid
Purity: >98%, HPLC
Solubility: Stock solution in DMSO (up to 500 mM), then dilute to appropriate concentration in aqueous buffer with final DMSO concentration <5%
Stability: >6 months at -30C
Spectral Information: 1H-NMR (400 MHz, CDCl3): δ 5.42 (s, 1H), 3.41 (d, J= 4.0 Hz, 2H), 2.75?1.72 (m, 16H), 1.68?1.45 (m, 6H). 13C-NMR (100 MHz, CDCl3): δ 204.9, 204.4, 197.0, 189.2, 104.2, 84.4, 84.1, 69.1, 68.9, 58.5, 49.1, 41.8, 39.9, 30.1, 29.6, 28.5, 26.4, 26.2, 26.1, 24.7, 18.8, 18.7. ESI-MS, m/z for C11H14O2: calculated, 178.23; observed, 179.1 [M + H+]
Storage: Room temperature for short-term, -30 oC for long term storage.
Shipped: Dry ice

From the laboratory of Kate Carroll, PhD, The Scripps Research Institute.
  1. Paulsen, C.E. et al. Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity, Nat. Chem. Biol. 8 (2012) 57–64.
  2. Yang, J. et al. Site-specific mapping and quantification of protein S-sulphenylation in cells, Nat. Commun. 5 (2014) 4776-4787.
  3. Gupta, V and Carroll, K.S. Sulfenic acid chemistry, detection and cellular lifetime, Biochimica et Biophysica Acta 1840 (2014) 847-875.
  4. Akter S, Huang J, Bodra N, De Smet B, Wahni K, Rombaut D, Pauwels J, Gevaert K, Carroll K, Van Breusegem F, Messens J. DYn-2 Based Identification of Arabidopsis Sulfenomes. Mol Cell Proteomics. 2015 May;14(5):1183-200. doi: 10.1074/mcp.M114.046896. View article
  5. Heppner DE, Dustin CM, Liao C, Hristova M, Veith C, Little AC, Ahlers BA, White SL, Deng B, Lam YW, Li J, van der Vliet A. Direct cysteine sulfenylation drives activation of the Src kinase. Nat Commun. 2018 Oct 30;9(1):4522. View Article
  6. Dustin CM, Hristova M, Schiffers C, van der Vliet A. Proteomic Methods to Evaluate NOX-Mediated Redox Signaling. Methods Mol Biol. 2019;1982:497-515. View Article

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