Clone: F16 P2 D8.
Background: The cytochrome P450 proteins (CYPs) are monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. P450 enzymes are classified into subfamilies based on their sequence similarities. CYP2A6 is a liver enzyme that metabolizes a number of drugs and a variety of procarcinogens, though it is primarily responsible for the metabolism of nicotine, the major addictive agent in tobacco. CYP2A6 inactivates nicotine to cotinine, and then cotinine to 3-hydroxycotinine. Differences in CYP2A6 genotypes are related to nicotine dependence, and may influence smoking habits and withdrawal symptoms in individuals that are quitting smoking. This suggests that an individualized smoking cessation program may be designed based on CYP2A6 genotypes.
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Positive Control: Normal human liver tissue.
Purification Method: Protein A/G Chromatography.
Source: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with Synthetic peptide conjugated to ovalbumin derived from the C-terminus of CYP2A6 and mouse myeloma Ag8563 cells. Antigen identical in CYP2A6, 2A7 and 2A13.
References: 1. Kumarakulasingham M, et al. (2005). Cytochrome p450 profile of colorectal cancer: identification of markers of prognosis. Clin Cancer Res. May 15;11(10):3758-65
2. Swan, G.E. (2005). Nicotine metabolism: the impact of CYP2A6 on estimate of additive genetic influence. Pharmacogenet. Genomics 15(2);115-125
3. Higashi, E., et al. (2007). Inhibitory effects of neurotransmitters and steroids on human CYP2A6. Drug Metab Dispos. 35(4); 508-514
4. Audrain-McGovern, J., et al. (2007). The role of CYP2A6 in the emergence of nicotine dependence in adolescents. 119(1);264-274.
UniProt: P05177.
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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