DCP-Rho1 is cell permeable and is selectively reactive with sulfenic acids. It can be detected on proteins by fluorescence (see Poole et al., 2007) or in fixed cells by fluorescence imaging (see Klomsiri et al., 2014).
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-Rho1 can be used to effectively detect the formation of cysteine sulfenic acid in the redox regulation of proteins, and with the presence of a rhodamine moiety, DCP-Rho1 is compatible with several techniques and forms of analysis post-labeling.
|Product Type:||Small Molecule|
|Molecular Weight:||743.3 g/mol (DCP-Rho1·HCl)|
|Purity:||85% by NMR, 15% is unreactive precursor (see reference 1 below)|
|Solubility:||DMSO, ethanol, 50% ethanol (up to 200 mM)|
|Spectral Information:||?max, Ex=560nm, ?max, Em=581nm Molar extinction coefficient ~70,000 M-1cmin phosphate buffer at pH 7|
|Storage:||-20C for long term storage|
Unreactive precursor has been tested and shown not to label cells under same conditions as DCP-Rho1, as shown in reference 1 below.
DCP-Rho1 can be detected on proteins by fluorescence (see Poole et al., 2007) or in fixed cells by fluorescence imaging (see Klomsiri et al., 2014).
Use at 5 to 10 micromolar applied to cells growing in wells, volume per sample up to ~0.5 ml (thus 5 nmol or 3.5 microgram per well).
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