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.
Highlights:
- 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.
DYn-2-d6 is a deuterated version of DYn-2, a chemoselective probe for detecting sulfenylated proteins in intact cells.
Highlights:
- 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 |
|---|
Specifications
| 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 |
Provider
From the laboratory of Kate Carroll, PhD, The Scripps Research Institute.
References
- Gupta, V. and Carroll, K.S. Sulfenic acid chemistry, detection and cellular lifetime Biochimica et Biophysica Acta 1840 (2014) 847-875.
- Paulsen, C.E. et al. Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity, Nat. Chem. Biol. 8 (2012) 57-64.
- Yang, J. et al. Site-specific mapping and quantification of protein S-sulphenylation in cells, Nat. Commun. 5 (2014) 4776-4787.
- 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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