DCP-Alkyne
DCP-Alkyne is dimedone based and contains an alkyne group allowing for selective conjugation via “click” chemistry or Staudinger ligation to azide linked detectable reagents such as biotin or common fluorophores.
Highlights:
- Stable, reproducible binding to cysteine sulfenic acid (-SOH) at pH 6.0-8.0
- Highly customizable - Alkyne group allows for use in a variety of analytical techniques
- Great for in vitro and in vivo applications
- Compatible with WB, ELISA, and Affinity Isolation
Redox-sensitive cysteine residues in proteins may serve as important components of oxidative signaling or sensors of oxidative stress. Cysteine sulfenic acid modification is an emerging area of interest for those studying biological signal transduction within the cell.
Cysteine sulfenic acid formation in proteins results from the oxidative modification of susceptible cysteine residues by mild oxidizing agents such as hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. These sulfenic acid modified proteins can be identified by their ability to form adducts with dimedone, but this reagent provides no spectral or affinity tag to such adduct to allow for later analysis. DCP-Alkyne can be used to effectively detect the formation of cysteine sulfenic acid in the redox regulation of proteins. The alkyne group can be used for selective conjugation to phosphine- or alkynyl- containing reagents such as biotin or common fluorophores for desired analytical techniques, and can be used to label protein sulfenic acids in cellular proteins, either by in situ labeling of intact cells or by labeling at the time of lysis.
From the laboratories of S. Bruce King, PhD and Leslie B. Poole, PhD, Wake Forest School of Medicine.
Part of The Investigator's Annexe program.
DCP-Alkyne is dimedone based and contains an alkyne group allowing for selective conjugation via “click” chemistry or Staudinger ligation to azide linked detectable reagents such as biotin or common fluorophores.
Highlights:
- Stable, reproducible binding to cysteine sulfenic acid (-SOH) at pH 6.0-8.0
- Highly customizable - Alkyne group allows for use in a variety of analytical techniques
- Great for in vitro and in vivo applications
- Compatible with WB, ELISA, and Affinity Isolation
Redox-sensitive cysteine residues in proteins may serve as important components of oxidative signaling or sensors of oxidative stress. Cysteine sulfenic acid modification is an emerging area of interest for those studying biological signal transduction within the cell.
Cysteine sulfenic acid formation in proteins results from the oxidative modification of susceptible cysteine residues by mild oxidizing agents such as hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. These sulfenic acid modified proteins can be identified by their ability to form adducts with dimedone, but this reagent provides no spectral or affinity tag to such adduct to allow for later analysis. DCP-Alkyne can be used to effectively detect the formation of cysteine sulfenic acid in the redox regulation of proteins. The alkyne group can be used for selective conjugation to phosphine- or alkynyl- containing reagents such as biotin or common fluorophores for desired analytical techniques, and can be used to label protein sulfenic acids in cellular proteins, either by in situ labeling of intact cells or by labeling at the time of lysis.
From the laboratories of S. Bruce King, PhD and Leslie B. Poole, PhD, Wake Forest School of Medicine.
Part of The Investigator's Annexe program.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Small Molecule |
| Name: | DCP-Alkyne (aka DYn-2) |
| Chemical Formula: | C11H14O2 |
| Source: | Synthetic |
| Molecular Weight: | 178.2 g/mol |
| Format: | off-white solid |
| Purity: | >95% by NMR |
| Solubility: | DMSO, ethanol, 50% ethanol (up to 100 mg/ml) |
| Storage: | -20C for long term storage |
| Shipped: | Ambient temperature |
- Paulsen, C.E., Truong, T.H., Garcia, F.J., Homann, A., Gupta, V., Leonard, S.E. & Carroll, K.S. Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity. Nat Chem Biol 8, 57-64 (2011).
- Wages PA. Detecting Protein Sulfenylation in Cells Exposed to a Toxicant. Curr Protoc Toxicol. 2017 Feb 1;71:17.18.1-17.18.12. View Article
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