Clone: 3B8C1
Background: P450 enzymes constitute a family of monooxygenase enzymes that are involved in the metabolism of a wide array of endogenous and xenobiotic compounds. Several P450 enzymes have been classified by sequence similarities as members of the CYP1A and CYP2A subfamilies. NADPH cytochrome 450 reductase is a microsomal enzyme responsible for the transfer of electrons from NADPH to cytochrome P450 enzymes during the P450 catalytic cycle. NADPH cytochrome P450 reductase is localized to the endoplasmic reticulum where it is also able to transfer electrons to heme oxygenase and cytochrome 5. NADPH cytochrome P450 reductase is structurally related to two separate flavoprotein families, ferredoxin nucleotide reductase (FNR) and flavodoxin. Electron transfer of NADPH cytochrome P450 reductase requires the binding of two flavin cofactors, FAD and FMN, to the FNR and flavodoxin domains, respectively.
Positive Control: Normal human liver sections
Immunogen: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with rat cytochrome p450 proteins and mouse myeloma Ag8563 cells.
Purification Method: Protein A/G Chromatography
Concentration: See vial for concentration
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide
References: 1. Peng, W.X., et al. (2003). Evidence of the involvement of human liver microsomes CYP1A2 in the mono-hydroxylation of daidzein. Clin. Chim. Acta. 334(1-2); 77-85.2. Hu, M., et al. Identification of CYP1A2 as the main isoform for the phase I hydroxylated metabolism of genistein and a prodru converting enzyme of methylated isoflavones. Drug Metab Dispos. 31(7); 924-931.3. Wei, C., et al. CYP1A2 is expressed along with CYP1A1 in the human lung. Cancer Lett. 171(1);113-120.
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.