CYP3A4 Protein, Human (Cell-Free, His)

CYP3A4 Protein, a cytochrome P450 monooxygenase, catalyzes diverse substrate metabolism, including sterols, hormones, and fatty acids. Mechanistically, it employs molecular oxygen for hydroxylation, impacting androgen metabolism, cholesterol, and retinoid pathways. Notably, it contributes to drug metabolism and regulates vitamin D catabolism, essential for calcium homeostasis. CYP3A4 Protein, Human (Cell-Free, His) is the recombinant human-derived CYP3A4 protein, expressed by E. coli Cell-free, with N-10*His labeled tag. The total length of CYP3A4 Protein, Human (Cell-Free, His) is 502 a.a., with molecular weight of 63.3 kDa.

The CYP3A4 protein, a cytochrome P450 monooxygenase, is intricately involved in the metabolism of a diverse array of substrates, including sterols, steroid hormones, retinoids, and fatty acids. Mechanistically, it utilizes molecular oxygen to insert one oxygen atom into a substrate and reduces the second into a water molecule, with two electrons supplied by NADPH via cytochrome P450 reductase. CYP3A4 catalyzes the hydroxylation of carbon-hydrogen bonds and exhibits high catalytic activity in the formation of hydroxyestrogens from estrone and 17beta-estradiol. Notably, it plays a crucial role in androgen metabolism, contributing to the oxidative deactivation of testosterone and the formation of less biologically active hydroxytestosterones. Furthermore, CYP3A4 is instrumental in the metabolism of cholesterol, contributing to the formation of hydroxycholesterols and likely participating in cholesterol degradation and bile acid biosynthesis. The protein also catalyzes bisallylic hydroxylation of polyunsaturated fatty acids, epoxidation of double bonds in polyunsaturated fatty acids, and the metabolism of endocannabinoid arachidonoylethanolamide. Additionally, CYP3A4 plays a role in retinoid metabolism, displaying high catalytic activity in the oxidation of all-trans-retinol to all-trans-retinal, a key step in the biosynthesis of all-trans-retinoic acid. Moreover, it is responsible for the oxidative metabolism of various xenobiotics, serving as a major contributor to drug metabolism and playing a role in vitamin D catabolism and calcium homeostasis by catalyzing the inactivation of the active hormone calcitriol.

Human

E. coli Cell-free

N-10*His

P08684 (A2-A503)

1576

ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA

63.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.