Stability 2 years
Storage -80°C
Cytochrome P450 1B1 (human) Yeast Reductase is found mainly in extrahepatic tissues and is overexpressed in a smorgasbord of human tumors. In contrast, V79 cells stably expressing human P450 1B1 generated exclusively DB[a,l]PDE-DNA adducts. Differences in the total level of DNA binding were also observed.
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).
More about: Cytochrome P450 1B1 (human) Yeast Reductase sale
Read more: Medicine raw materials
No comments:
Post a Comment