Anti-Human CYP1A1 DyLight® 488 conjugated Antibody, Carrier-free

CYP1A1 is involved in phase I xenobiotic and drug metabolism (one substrate of it is theophylline). It is inhibited by fluoroquinolones and macrolides and induced by aromatic hydrocarbons. CYP1A1 is also known as AHH (aryl hydrocarbon hydroxylase). It is involved in the metabolic activation of aromatic hydrocarbons (polycyclic aromatic hydrocarbons, PAH), for example, benzo (a)pyrene (BP), by transforming it to an epoxide. In this reaction, the oxidation of benzo[a]pyrene is catalysed by CYP1A1 to form BP-7,8-epoxide, which can be further oxidized by epoxide hydrolase (EH) to form BP-7,8-dihydrodiol. Finally CYP1A1 catalyses this intermediate to form BP-7,8-dihydrodiol-9,10-epoxide, which is the ultimate carcinogen. However, an in vivo experiment with gene-deficient mice has found that the hydroxylation of benzo (a)pyrene by CYP1A1 can have an overall protective effect on the DNA, rather than contributing to potentially carcinogenic DNA modifications. This effect is likely due to the fact that CYP1A1 is highly active in the intestinal mucosa, and thus inhibits infiltration of ingested benzo (a)pyrene carcinogen into the systemic circulation.

E.coli-derived human CYP1A1 recombinant protein (Position: H183-D320). Human CYP1A1 shares 81.2% amino acid (aa) sequence identity with both mouse and rat CYP1A1.

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

1. Beresford AP (1993). "CYP1A1: friend or foe?". Drug Metabolism Reviews 25 (4): 503–17. 2. Uno, S (2004). "Oral exposure to benzo[a]pyrene in the mouse: detoxication by inducible cytochrome P450 is more important than metabolic activation.". Mol Pharmacol 65 (5): 1225–37.