DCP-N3
DCP-N3 is dimedone based and contains an azide group allowing for selective conjugation to phosphine- or alknyl- containing reagents such as biotin or common fluorophores.
Features:
- Stable, reproducible binding to cysteine sulfenic acid (-SOH) at pH 6.0-8.0
- Highly customizable - Azide 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-N3 can be used to effectively detect the formation of cysteine sulfenic acid in the redox regulation of proteins. The azide 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 laboratory of Leslie B. Poole, PhD, Wake Forest School of Medicine.
DCP-N3 is dimedone based and contains an azide group allowing for selective conjugation to phosphine- or alknyl- containing reagents such as biotin or common fluorophores.
Features:
- Stable, reproducible binding to cysteine sulfenic acid (-SOH) at pH 6.0-8.0
- Highly customizable - Azide 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-N3 can be used to effectively detect the formation of cysteine sulfenic acid in the redox regulation of proteins. The azide 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 laboratory of Leslie B. Poole, PhD, Wake Forest School of Medicine.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Small Molecule |
| Name: | DCP-N3 ( 4-(azidopropyl)cyclohexane-1,3-dione) |
| Chemical Formula: | C9H13N3O2 |
| Source: | synthetic |
| Molecular Weight: | 195.2 g/mol |
| Format: | solid |
| Purity: | >98% pure |
| Solubility: | At least 500 mM in DMSO, at least 5 mg/ml in acetonitrile |
| Stability: | stable > 1 year at -20 degC |
| Spectral Information: | No visible absorbance |
| Storage: | room temperature for short term, -20 degC for long term |
Stock solution in DMSO can be added to cell lysis buffer, preferrably keeping final [DMSO] < 2% for labeling proteins. Can be dissolved in acetonitrile to prepare aliquots and redry.
- Leonard, S.E., Reddie, K.G. & Carroll, K.S. Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem Biol 4, 783-99 (2009)
- Klomsiri, C., Nelson, K.J., Bechtold, E., Soito, L., Johnson, L.C., Lowther, W.T., Ryu, S.E., King, S.B., Furdui, C.M. & Poole, L.B. Use of dimedone-based chemical probes for sulfenic acid detection: evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods Enzymol 473, 77-94 (2010)
- Nelson, K.J., Klomsiri, C., Codreanu, S.G., Soito, L., Liebler, D.C., Rogers, L.C., Daniel, L.W. & Poole, L.B. Use of dimedone-based chemical probes for sulfenic acid detection; methods to visualize and identify labeled proteins. Methods Enzymol 473, 95-115 (2010)
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