DYn-2-d6 Sulfenic Acid Probe

DYn-2-d6 is a deuterated version of DYn-2, a chemoselective probe for detecting sulfenylated proteins in intact cells.


  • Consists of 1,3-cyclohexanedione coupled to an alkyne moiety by a fully deuterated 3-carbon spacer
  • Cyclohexanedione group selectively reacts with protein sulfenic acid modifications
  • Alkyne group of DYn-2-d6 can be detected using azide-bearing tags by standard click chemistry
  • Can be used with non-deuterated analog DYn-2 (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-d6 Sulfenic Acid Probe, 10mg
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DYn-2-d6 Sulfenic Acid Probe, 25mg
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DYn-2-d6 Sulfenic Acid Probe, 1mg
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DYn-2-d6 Sulfenic Acid Probe, 5mg
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Product Type: Small Molecule
Name: DYn-2-d6
Chemical Formula: C11H8D6O2
Molecular Weight: 184.27
Format: Yellow Solid
Purity: > 98%, HPLC
Solubility: DMSO
Stability: >6 months at -20C
Spectral Information: 1H-NMR (400 MHz, CDCl3): δ 5.43 (s, 1H), 3.41 (d, J = 8.0 Hz, 2H), 2.75 ? 2.28 (m, 6H), 2.18 ? 2.00 (m, 2H), 1.95 (s, 1H), 1.94 (s, 1H), 1.82 ? 1.71 (m, 1H), 1.65 ? 1.50 (m,1H); 13C-NMR (100 MHz, CDCl3): δ 204.6, 204.1, 196.6, 188.8, 104.0, 84.1, 83.8, 68.9, 68.6, 58.2, 48.7, 41.4, 39.6, 29.9, 25.9, 24.4; LC-MS: m/z for C11H8D6O2calculated: 184.27; observed: 185.15 (M+ + 1, 100%)
Storage: -20C
Shipped: Dry ice

From the laboratory of Kate Carroll, PhD, The Scripps Research Institute.
  1. Gupta, V. and Carroll, K.S. Sulfenic acid chemistry, detection and cellular lifetime Biochimica et Biophysica Acta 1840 (2014) 847-875.
  2. Paulsen, C.E. et al. Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity, Nat. Chem. Biol. 8 (2012) 57-64.
  3. Yang, J. et al. Site-specific mapping and quantification of protein S-sulphenylation in cells, Nat. Commun. 5 (2014) 4776-4787.
  4. Yang J, Gupta V, Tallman KA, Porter NA, Carroll KS, Liebler DC. Global, in situ, site-specific analysis of protein S-sulfenylation. Nat Protoc. 2015 Jul;10(7):1022-37. View Article

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