Recombinant Rat CYP2F2 protein

CYP2F2. a member of the cytochrome P450 superfamily, is a membrane-bound monooxygenase enzyme primarily involved in the metabolism of endogenous and exogenous compounds. It is predominantly expressed in the lung and liver tissues of certain species, including mice, and plays a critical role in the bioactivation of toxicants and procarcinogens. Unlike some human P450 isoforms (e.g., CYP2A13), CYP2F2 exhibits species-specific expression patterns, making it a valuable model for studying pulmonary xenobiotic metabolism and toxicity mechanisms. Its enzymatic activity is linked to the metabolic activation of environmental pollutants like naphthalene, styrene, and 3-methylindole, which can cause lung injury through the generation of reactive intermediates.

Recombinant CYP2F2 protein is engineered using heterologous expression systems such as Escherichia coli or insect cell lines (e.g., baculovirus/Sf9), often co-expressed with NADPH-cytochrome P450 reductase to restore catalytic functionality. This recombinant form enables detailed in vitro studies on substrate specificity, enzyme kinetics, and inhibitor interactions without interference from other metabolic pathways present in vivo. Structural and functional analyses of recombinant CYP2F2 have provided insights into its unique substrate-binding pocket architecture, explaining its preference for small hydrophobic molecules. Researchers also utilize this protein to investigate interspecies differences in toxicant metabolism, particularly relevant for extrapolating rodent-based toxicology data to human risk assessment. Additionally, CYP2F2 serves as a tool for identifying potential drug candidates that might undergo bioactivation into toxic metabolites, contributing to safety evaluations during pharmaceutical development. Its study remains crucial for understanding chemical-induced pulmonary damage and optimizing predictive toxicological models.