Cytochrome P450 1B1 (human) Yeast Reductase
Stability : 2 years
Human cytochrome P450 1B1 (CYP1B1) is found mainly in extrahepatic tissues and is overexpressed in a variety of human tumors. Metabolic activation of 17β-estradiol (E2) to 4-hydroxy E2 by CYP1B1 has been postulated to be an important factor in mammary carcinogenesis. The inhibition of recombinant human CYP1B1 by 2,2′,4,6′-tetramethoxystilbene (TMS) was investigated using either the Escherichia coli membranes of recombinant human CYP1B1 coexpressed with human NADPH-P450 reductase or using purified enzyme. 2,2′,4,6′-TMS showed potent and selective inhibition of ethoxyresorufin O-deethylation (EROD) activity of CYP1B1 with IC50 values of 2 nM. 2,2′,4,6′-TMS exhibited 175-fold selectivity for CYP1B1 over CYP1A1 (IC50, 350 nM) and 85-fold selectivity for CYP1B1 over CYP1A2 (IC50, 170 nM). However, inhibition of human NADPH-P450 reductase activity by 2,2′,4,6′-TMS was negligible. The modes of inhibition by 2,2′,4,6′-TMS were noncompetitive for CYP1A1 and CYP1B1.
Storage : -80°C
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