Anti-Cytochrome P450 1A2/CYP1A2 Antibody Picoband® Fluoro647 Conjugated

CYP1A2 (Cytochrome P450, Subfamily I, Polypeptide 2) is a member of the cytochrome P450 mixed-function oxidase system and is involved in the metabolism of xenobiotics in the body. CYP1A2 is a member of the cytochrome P450 superfamily of enzymes. In humans, the CYP1A2 enzyme is encoded by the CYP1A2 gene. CYP1A2 localizes to the endoplasmic reticulum and its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), some of which are found in cigarette smoke. The CYP1A2 gene encodes a P450 enzyme involved in O-deethylation of phenacetin. Ikeya et al. (1989) found that the human CYP1A2 gene spans almost 7.8 kb and contains 7 exons. The CYP1A2 gene is mapped on 15q24.1. CYP1A2 accounts for nearly 15% of the cytochrome P450 in the human liver. CYP1A2 displays higher activity in men than in women, and is inhibited by oral contraceptives. Inducers of CYP1A2 include cruciferous vegetables. Cigarette smoking has also been shown to increase CYP1A2 activity. Expression of CYP1A2 appears to be induced by various dietary constituents.

E.coli-derived human CYP1A2 recombinant protein (Position: H185-D320) . Human CYP1A2 shares 69.9% and 72.1% amino acid (aa) sequence identity with mouse and rat CYP1A2, respectively.

Cancer, Cancer Metabolism, Cardiovascular, Cytochromes, Drug Metabolism, Lipases, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathways, Metabolism, Mitochondrial Metabolism, Pathways and Processes, Signal Transduction

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. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O- deethylation of phenacetin. .

1. Browning, S. L., Tarekegn, A., Bekele, E., Bradman, N., Thomas, M. G. CYP1A2 is more variable than previously thought: a genomic biography of the gene behind the human drug-metabolizing enzyme. Pharmacogenet. Genomics 20: 647-664, 2010. 2. Ikeya, K., Jaiswal, A. K., Owens, R. A., Jones, J. E., Nebert, D. W., Kimura, S. Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. Molec. Endocr. 3: 1399-1408, 1989. 3. Nakajima, M., Yokoi, T., Mizutani, M., Kinoshita, M., Funayama, M., Kamataki, T. Genetic polymorphism in the 5-prime-flanking region of human CYP1A2 gene: effect on theCYP1A2 inducibility in humans. J. Biochem. 125: 803-808, 1999.