Cytochrome P450 2C9 (CYP2C9) is a key hepatic enzyme involved in the metabolism of approximately 15-20% of clinically used drugs, including warfarin, phenytoin, and nonsteroidal anti-inflammatory drugs. As a member of the cytochrome P450 superfamily, it plays a critical role in phase I drug metabolism through oxidation reactions. Genetic polymorphisms in the CYP2C9 gene, particularly the *2 and *3 alleles, significantly influence enzyme activity, leading to interindividual variability in drug efficacy and toxicity. This has made CYP2C9 a major focus in pharmacogenetic studies and personalized medicine.
Antibodies targeting CYP2C9 are essential tools for investigating its expression, localization, and function in both research and clinical settings. They enable detection of CYP2C9 protein levels in tissues (e.g., liver biopsies) via techniques like Western blotting, immunohistochemistry, or immunofluorescence. Such antibodies also support studies on enzyme regulation under pathological conditions (e.g., liver disease) or drug-induced modulation. Commercially available antibodies are typically raised against specific epitopes of the human CYP2C9 protein, with validation for species reactivity and application compatibility. In clinical diagnostics, CYP2C9 antibodies may assist in assessing protein expression patterns to complement genetic testing, particularly when genotype-phenotype correlations are ambiguous. However, cross-reactivity with other CYP isoforms remains a challenge, necessitating rigorous validation for specificity. Overall, CYP2C9 antibodies contribute to advancing drug development, toxicology research, and precision medicine strategies.