Human CYP2A6 (Cytochrome P450 2A6) ELISA Kit
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Product specifications
| Category | ELISA Kits |
| Reactivity | Human |
| Detection Method | Colorimetric |
| Assay Data | 4 hours |
| Assay Type | Sandwich ELISA, Double Antibody |
| Test Range | 1.563-100ng/ml |
| Sensitivity | 0.938ng/ml |
| Size 1 | 96T |
| Tested Applications | ELISA |
| Sample Type | cell or tissue lysate, Other liquid samples |
| Availability | Shipped within 10-14 working days. |
| Storage | 2-8 °C for 12 months |
| UniProt ID | P11509 |
| Alias | Cytochrome P450 2A6, 1,4-cineole 2-exo-monooxygenase, CYPIIA6, Coumarin 7-hydroxylase, Cytochrome P450 IIA3, Cytochrome P450(I, CYP2A6, CYP2A3 |
| Background | Elisa kits for CYP2A6 |
| Status | RUO |
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Human CYP2A6 (Cytochrome P450 2A6) ELISA Kit
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CYP2A6 antibody
Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-cineole 2-exo-monooxygenase. Possesses low phenacetin O-deethylation activity.
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Cytochrome P450 2A6 (CYP2A6) Antibody
CYP2A6 Antibody is a Rabbit Polyclonal antibody against CYP2A6. This gene, CYP2A6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and its expression is induced by phenobarbital. The enzyme is known to hydroxylate coumarin, and also metabolizes nicotine, aflatoxin B1, nitrosamines, and some pharmaceuticals. Individuals with certain allelic variants are said to have a poor metabolizer phenotype, meaning they do not efficiently metabolize coumarin or nicotine. This gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. The gene was formerly referred to as CYP2A3; however, it has been renamed CYP2A6.
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