7-EthoxycoumarinCAS# 31005-02-4 |
Quality Control & MSDS
Number of papers citing our products
Chemical structure
3D structure
| Cas No. | 31005-02-4 | SDF | Download SDF |
| PubChem ID | 35703 | Appearance | Cryst. |
| Formula | C11H10O3 | M.Wt | 190.2 |
| Type of Compound | Coumarins | Storage | Desiccate at -20°C |
| Solubility | Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc. | ||
| Chemical Name | 7-ethoxychromen-2-one | ||
| SMILES | CCOC1=CC2=C(C=C1)C=CC(=O)O2 | ||
| Standard InChIKey | LIFAQMGORKPVDH-UHFFFAOYSA-N | ||
| General tips | For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months. We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months. Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it. |
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| About Packaging | 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial. 2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial. 3. Try to avoid loss or contamination during the experiment. |
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| Shipping Condition | Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request. | ||
| Description | The oxidation of 7-Ethoxycoumarin, a typical human P450 substrate, is catalyzed by both wild-type and mutant forms of CYP102A1. |
| Targets | P450 (e.g. CYP17) |
| Kinase Assay | Generation of human metabolites of 7-ethoxycoumarin by bacterial cytochrome P450 BM3.[Pubmed: 18669587]Drug Metab Dispos. 2008 Nov;36(11):2166-70.Recently, wild-type and mutant forms of bacterial cytochrome P450 BM3 (CYP102A1) have been found to metabolize various drugs through reactions similar to those catalyzed by human cytochromes P450 (P450s). Therefore, it has been suggested that CYP102A1 may be used to produce large quantities of the metabolites of human P450-catalyzed reactions. |
7-Ethoxycoumarin Dilution Calculator
7-Ethoxycoumarin Molarity Calculator
| 1 mg | 5 mg | 10 mg | 20 mg | 25 mg | |
| 1 mM | 5.2576 mL | 26.2881 mL | 52.5762 mL | 105.1525 mL | 131.4406 mL |
| 5 mM | 1.0515 mL | 5.2576 mL | 10.5152 mL | 21.0305 mL | 26.2881 mL |
| 10 mM | 0.5258 mL | 2.6288 mL | 5.2576 mL | 10.5152 mL | 13.1441 mL |
| 50 mM | 0.1052 mL | 0.5258 mL | 1.0515 mL | 2.103 mL | 2.6288 mL |
| 100 mM | 0.0526 mL | 0.2629 mL | 0.5258 mL | 1.0515 mL | 1.3144 mL |
| * Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations. | |||||
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Generation of human metabolites of 7-ethoxycoumarin by bacterial cytochrome P450 BM3.[Pubmed:18669587]
Drug Metab Dispos. 2008 Nov;36(11):2166-70.
Recently, wild-type and mutant forms of bacterial cytochrome P450 BM3 (CYP102A1) have been found to metabolize various drugs through reactions similar to those catalyzed by human cytochromes P450 (P450s). Therefore, it has been suggested that CYP102A1 may be used to produce large quantities of the metabolites of human P450-catalyzed reactions. In this report, we show that the oxidation of 7-Ethoxycoumarin, a typical human P450 substrate, is catalyzed by both wild-type and mutant forms of CYP102A1. Two major products were produced as a result of O-deethylation and 3-hydroxylation reactions. These results demonstrate that CYP102A1 mutants catalyze the same reactions as human P450s. High noncompetitive intermolecular kinetic deuterium isotope effects were observed for 7-Ethoxycoumarin O-deethylation in the CYP102A1 system. These results suggest that there is a common mechanism for the oxidation reactions catalyzed by both the bacterial CYP102A1 and human P450 enzymes.
