DYn-2

Mild oxidation can convert the sulfhydryl group of cysteine residues on proteins to cysteine-sulfenic acid derivatives (Cys-SOH).¹ Protein sulfenylation, then, is a post-translational modification that is relevant to redox signaling. DYn-2 is a chemoselective probe for detecting sulfenylated proteins in intact cells.² DYn-2 consists of 1,3-cyclohexanedione coupled to an alkyne moiety by a 3-carbon spacer. The cyclohexanedione group selectively reacts with protein sulfenic acid modifications.² The alkyne group of DYn-2 can then be detected using azide-bearing tags by standard click chemistry. This approach offers superior sensitivity relative to using azide-modified probes with alkynyl detection tags.³

WARNING This product is not for human or veterinary use.

1. Kettenhofen, N.J., and Wood, M.J. Formation, reactivity and detection of protein sulfenic acids. Chem. Res. Toxicol. 23(11), 1633-1646 (2010).

2. Paulsen, C.E., Truong, T.H., Garcia, F.J., et al. Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity. Nat. Chem. Biol. 8(1), 57-64 (2012).

3. Charron, G., Zhang, M.M., Yount, J.S., et al. Robust fluorescent detection of protein fatty-acylation with chemical reporters. J. Am. Chem. Soc. 131(13), 4967-4975 (2009).