CYP3A4 Activity Assay Kit (Fluorometric)
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(4 Publications)
CYP3A4 Activity Assay Kit (Fluorometric) (ab211076) allows rapid measurement of native or recombinant CYP3A4 activity in biological samples such as liver microsomes.
View Alternative Names
Cytochrome P450 3A43, CYP3A43
- FuncS
Supplier Data
Functional Studies - CYP3A4 Activity Assay Kit (Fluorometric) (AB211076)
Reaction kinetics of fluorogenic substrate metabolism in human liver microsomes (0.05 mg/mL) at 37°C in the presence and absence of the CYP3A4 inhibitor Ketoconazole ("no inhibitor" reaction contained a final concentration of 0.6% acetonitrile).
- FuncS
Supplier Data
Functional Studies - CYP3A4 Activity Assay Kit (Fluorometric) (AB211076)
Typical Resorufin standard calibration curve. One mole of resorufin corresponds to the metabolism of one mole of CYP3A4 substrate.
- FuncS
Supplier Data
Functional Studies - CYP3A4 Activity Assay Kit (Fluorometric) (AB211076)
Specific activity of CYP3A4 in pooled human liver microsomes (0.05 mg/mL).
Reactivity data
Product details
CYP3A4 Activity Assay Kit (Fluorometric) (ab211076) allows rapid measurement of native or recombinant CYP3A4 activity in biological samples such as liver microsomes. The assay utilizes a non-fluorescent CYP3A4 substrate that is converted into a highly fluorescent metabolite detected in the visible range (Ex/Em = 535/587 nm), ensuring a high signal-to-background ratio with little interference by autofluorescence. CYP3A4 specific activity is calculated by running parallel reactions in the presence and absence of the potent inhibitor Ketoconazole and subtracting any residual activity detected with the inhibitor present.
The kit contains enough reagents to perform 100 sets of paired reactions (in presence / absence of inhibitor).
This product is manufactured by BioVision, an Abcam company and was previously called K701 Cytochrome P450 3A4 (CYP3A4) Activity Assay Kit (Fluorometric). K701-200 is the same size as the 200 test size of ab211076.
Cytochrome P450 3A4 (CYP3A4, EC 1.14.13.157) is a member of the cytochrome P450 monooxidase (CYP) family of microsomal xenobiotic metabolism enzymes. CYPs are membrane-bound hemeproteins responsible for Phase I biotransformation reactions, in which lipophilic drugs and other xenobiotic compounds are transformed to more hydrophilic products to facilitate excretion from the body. CYP3A4 is expressed in high levels in the liver and intestines, where it catalyzes oxidation of an extraordinarily wide variety of structurally distinct ligands. More than half of all small molecule drugs commonly used by humans are metabolized by CYP3A4. Inhibition of CYP3A4-mediated metabolism is a common cause of adverse drug/drug and drug/food interactions and toxicity. In addition, for drugs whose pharmacological activity requires metabolism from a pro-drug form, CYP3A4 inhibition can lead to decreased drug efficacy.
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CYP3A43 plays significant roles in drug metabolism and synthesis of cholesterol steroids and other lipids. It does not appear to be part of a larger enzyme complex functioning independently within cells. Its activity is essential in transforming various substances into metabolites some of which are inactive while others may remain active. The enzyme is important for modulating the pharmacokinetics of drugs which includes absorption distribution metabolism and excretion of pharmaceutical compounds.
Pathways
CYP3A43 is involved in the xenobiotic metabolism pathway alongside other enzymes like CYP3A4 and CYP3A5. This pathway facilitates the detoxification of potentially harmful compounds. Additionally CYP3A43 participates in the metabolism of endogenous substrates contributing to the homeostasis of steroid hormones. Within these pathways it interacts with other cytochrome P450 enzymes sharing substantial substrate overlaps and sometimes competing with CYP3A4 which significantly influences the effects and side effects of drugs.
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Publications (4)
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The Journal of biological chemistry 300:105633 PubMed38199567
2024
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RSC advances 12:19431-19444 PubMed35865562
2022
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Frontiers in bioengineering and biotechnology 10:826093 PubMed35372314
2022
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Journal of medicinal chemistry 64:8437-8446 PubMed34097831
2021
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