Recombinant Human Ces2e protein

Ces2e (carboxylesterase 2E) is a member of the carboxylesterase enzyme family, which plays critical roles in hydrolyzing ester- and amide-containing compounds, including xenobiotics and endogenous lipids. As a serine hydrolase, it shares structural homology with other CES isoforms, featuring a conserved catalytic triad (Ser-His-Glu) and a characteristic α/β-hydrolase fold. Ces2e is primarily expressed in metabolic tissues such as the liver and intestine, where it participates in Phase I drug metabolism, lipid regulation, and detoxification pathways. Its broad substrate specificity enables interactions with clinical drugs (e.g., chemotherapeutic prodrugs, antivirals), environmental toxins, and lipid-derived signaling molecules.

Recombinant Ces2e protein is engineered using heterologous expression systems like E. coli or mammalian cell lines, often fused with affinity tags (e.g., His-tag) for purification. This technology allows large-scale production of enzymatically active protein for functional studies. Research focuses on its role in drug activation/inactivation kinetics, with implications for personalized medicine. For instance, genetic polymorphisms in CES2E may influence individual responses to prodrugs like irinotecan. Additionally, Ces2e's involvement in lipid metabolism links it to metabolic disorders, driving interest in its regulatory mechanisms. Recombinant variants are also used to screen enzyme inhibitors or environmental pollutants, aiding toxicology assessments. Recent studies explore its potential as a biomarker or therapeutic target in cancers and fatty liver disease. However, functional redundancy among CES isoforms and tissue-specific expression patterns complicate its precise physiological characterization, underscoring the need for isoform-specific tools like recombinant proteins.