7-Ethoxycoumarin
(Synonyms: 7-乙氧基香豆素; 7-O-Ethylumbelliferone) 目录号 : GC49030
A CYP450 substrate
Cas No.:31005-02-4
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
7-Ethoxycoumarin is a substrate for cytochrome P450 (CYP).1 It undergoes O-deethylation by various CYP isoforms, including CYP1A1, -1A2, and -2B in mice and CYP2E1 in humans. 7-Ethoxycoumarin has been used in the functional characterization of CYPs in cats, rats, and isolated human cornea.2,3,4
1.Okamatsu, G., Komatsu, T., Kubota, A., et al.Identification and functional characterization of novel feline cytochrome P450 2AXenobiotica45(6)503-510(2015) 2.Kajbaf, M., Ricci, R., Zambon, S., et al.Contribution of rat intestinal metabolism to the xenobiotics clearanceEur. J. Drug Metab. Pharmacokinet.38(1)33-41(2013) 3.KÖlln, C., and Reichl, S.Cytochrome P450 activity in ex vivo cornea models and a human cornea constructJ. Pharm. Sci.105(7)2204-2212(2016)
| Cas No. | 31005-02-4 | SDF | |
| 别名 | 7-乙氧基香豆素; 7-O-Ethylumbelliferone | ||
| Canonical SMILES | O=C1C=CC2=CC=C(OCC)C=C2O1 | ||
| 分子式 | C11H10O3 | 分子量 | 190.2 |
| 溶解度 | DMF: 30 mg/ml,DMF:PBS (pH 7.2) (1:1): 0.50 mg/ml,DMSO: 15 mg/ml | 储存条件 | -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 5.2576 mL | 26.2881 mL | 52.5762 mL |
| 5 mM | 1.0515 mL | 5.2576 mL | 10.5152 mL |
| 10 mM | 0.5258 mL | 2.6288 mL | 5.2576 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Metabolism of 7-Ethoxycoumarin, flavanone and steroids by cytochrome P450 2C9 variants
Biopharm Drug Dispos 2017 Nov;38(8):486-493.PMID:28758225DOI:10.1002/bdd.2090.
CYP2C9 is a human microsomal cytochrome P450c (CYP). Much of the variation in CYP2C9 levels and activity can be attributed to polymorphisms of this gene. Wild-type CYP2C9 and mutants were coexpressed with NADPH-cytochrome P450 reductase in Escherichia coli. The hydroxylase activities toward 7-Ethoxycoumarin, flavanone and steroids were examined. Six CYP2C9 variants showed Soret peaks (450 nm) typical of P450 in reduced CO-difference spectra. CYP2C9.38 had the highest 7-Ethoxycoumarin de-ethylase activity. All the CYP2C9 variants showed lower flavanone 6-hydroxylation activities than CYP2C9.1 (the wild-type). CYP2C9.38 showed higher activities in testosterone 6β-hydroxylation, progesterone 6β-/16α-hydroxylation, estrone 11α-hydroxylation and estradiol 6α-hydroxylation than CYP2C9.1. CYP2C9.40 showed higher testosterone 17-oxidase activity than CYP2C9.1; CYP2C9.8 showed higher estrone 16α-hydroxylase activity and CYP2C9.12 showed higher estrone 11α-hydroxylase activity. CYP2C9.9 and CYP2C9.10 showed similar activities to CYP2C9.1. These results indicate that the substrate specificity of CYP2C9.9 and CYP2C9.10 was not changed, but CYP2C9.8, CYP2C9.12 and CYP2C9.40 showed different substrate specificity toward steroids compared with CYP2C9.1; and especially CYP2C9.38 displayed diverse substrate specificities towards 7-Ethoxycoumarin and steroids.
7-Ethoxycoumarin and 7-ethoxyresorufin O-deethylase in human foetal and adult liver: studies with monoclonal antibodies
Pharmacol Toxicol 1988 Jul;63(1):26-9.PMID:3261011DOI:10.1111/j.1600-0773.1988.tb00903.x.
The 7-Ethoxycoumarin and 7-ethoxyresorufin O-deethylase activities were investigated in the microsomal fractions from 5 human adult and 3 foetal livers and 5 human foetal adrenals. The enzyme activity expressed as pmol/min. per mg microsomal protein was higher with 7-ethoxyresorufin as substrate in all investigated specimens with average values (+/- S.E.M.) of 74 +/- 27, 13 +/- 3 and 12 +/- 1 in adult and foetal livers and foetal adrenals, respectively. Monoclonal antibodies raised against 3-methylchloranthrene or phenobarbital induced rat liver cytochrome P-450 were investigated with respect to their inhibiting effects on the rate of O-deethylation of both substrates in human adult liver. Only the monoclonal antibody against the 3-methylcholanthrene induced cytochrome P-450 inhibited the O-deethylation of 7-ethoxyresorufin to 64 to 79 percent of control values. The other antibody had no effect on this or the other O-deethylase activity. Thus, the 7-ethoxyresorufin O-deethylase is partly catalyzed in human adult liver by a cytochrome with an epitope that is recognized by the monoclonal antibody against 3-methylcholanthrene induced rat liver cytochrome P-450. With foetal liver the low activity of the enzyme became unmeasurable in the presence of this antibody.
7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes
Biochem Pharmacol 1996 Feb 9;51(3):313-9.PMID:8573198DOI:10.1016/0006-2952(95)02178-7.
7-Ethoxycoumarin O-deethylation has been used widely as a marker activity for assessing substrate specificities of cytochromes P450 (P450) in liver microsomes of mammals, and extensive studies have shown that in rats and mice the major catalysts are P450 1A1, 1A2, and 2B enzymes. In contrast to findings in experimental animal models, P450 2E1 has been reported to be a principal enzyme involved in 7-ethoxy-coumarin O-deethylation in human livers. In this study, we further examined the roles of individual forms of human P450 involved in 7-Ethoxycoumarin O-deethylation using microsomes from different human liver samples and from human lymphoblastoid cells expressing human P450 enzymes and purified P450 enzymes isolated from the membrane of Escherichia coli expressing modified P450 proteins. Kinetic analysis showed that there were at least two different enzymes involved in 7-Ethoxycoumarin O-deethylation in different human samples. Samples that contained high amounts of P450 2E1 in liver microsomes showed biphasic curves for O-deethylation with relatively high turnover numbers, whereas P450 1A2-rich samples tended to have low Km values with low Vmax values. Anti-human P450 2E1 antibodies inhibited markedly (P < 0.05) the 7-Ethoxycoumarin O-deethylation activities catalyzed by human liver microsomes particularly when examined at a high substrate concentration (200 microM). However, we also found that anti-P450 1A2 antibodies suppressed O-deethylation activities only at a low substrate concentration (10 microM). Recombinant human P450 1A2 was found to have a low Km value for 7-Ethoxycoumarin O-deethylation, whereas P450 2E1 showed a high Km value. Of the P450 enzymes examined, P450 1A1 gave the highest O-deethylation activities with a low Km value, although this enzyme is reported to be expressed extrahepatically in humans. Other human P450 enzymes, including P450 2A6, 2C10, 2D6, 3A4, and 3A5, did not show significant O-deethylation activities except that P450 2B6, a minor P450 component in human livers, was found to have a Vmax value similar to that of P450 1A2 and a Km value similar to that of P450 2E1. These results suggest that P450 1A2 is a low Km enzyme for 7-Ethoxycoumarin O-deethylation in human liver microsome, although it has a low Vmax value than P450 2E1.
[14C]7-Ethoxycoumarin metabolism by precision-cut rat hepatic slices
Drug Metab Dispos 1996 Apr;24(4):383-9.PMID:8801051doi
The metabolism of [14C]7-Ethoxycoumarin ([14C]7-EC) has been studied in rat liver slice cultures in vitro by using a direct radiometric high-pressure liquid chromatography method. [14C]7-EC was extensively biotransformed in these incubations to 7-hydroxycoumarin (7-OHC), 7-hydroxycoumarin glucuronide, and 7-hydroxycoumarin sulfate, as well as to a large number of previously unrecognized metabolites, the majority of which are sulfate conjugates. The liver slice [14C]7-EC metabolite profile was also very complex and seemed to be qualitatively similar to the medium metabolite profile. Quantitative comparisons, however, demonstrated that there was approximately two to five times more 7-OHC in the liver slice than in the medium, whereas 7-hydroxycoumarin sulfate, the most abundant metabolite in the medium, was present only at low levels in the liver slice. These data demonstrate that 7-OHC levels are considerably underestimated when only levels in the medium are considered. Total metabolite levels were approximately equal in the medium and liver slice after a 2-hr incubation, with considerably higher total metabolite levels present in the medium at the end of the incubation period (8 hr). Additional studies are needed to identify the structures of the previously unrecognized metabolites observed in this study and the enzymes responsible for their formation, as well as studies to define the metabolism of [14C]7-EC in other in vitro models by using tissue from humans and other animal species.
Novel Biotransformations of 7-Ethoxycoumarin by Streptomyces griseus
Appl Environ Microbiol 1983 Aug;46(2):468-74.PMID:16346369DOI:10.1128/aem.46.2.468-474.1983.
Biotransformation of 7-Ethoxycoumarin by Streptomyces griseus resulted in the accumulation of two metabolites which were isolated and identified as 7-hydroxycoumarin and 7-hydroxy-6-methoxycoumarin. A novel series of biotransformation reactions is implicated in the conversion of the ethoxycoumarin substrate to these products, including O-deethylation, 6-hydroxylation to form a 6,7-dihydroxycoumarin catechol, and subsequent O-methylation. Either 7-hydroxycoumarin or 6,7-dihydroxycoumarin was biotransformed to 7-hydroxy-6-methoxycoumarin by S. griseus. Trace amounts of the isomeric 6-hydroxy-7-methoxycoumarin were detected when 6,7-dihydroxycoumarin was used as the substrate. Efforts to obtain a cell-free catechol-O-methyltransferase enzyme system from S. griseus were unsuccessful. However, [methyl-C]methionine was used with cultures of S. griseus to form 7-hydroxy-6-[C]methoxycoumarin.