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 β5. 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.
Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with rat cytochrome p450 proteins and mouse myeloma Ag8563 cells.
Normal human liver sections
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Left: Western blot using CYP1A2 antibody (Cat. No. X2046M) on recombinant (2) CYP1B1, (3) CYP1A1 and (4) CYP1A2 (0.5 pmol per lane).
Right: Immunohistochemical staining of formalin-fixed, paraffin-embedded normal human liver tissue section.
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