Our enzymatic activity assays enable precise quantification of enzyme function, kinetics, and inhibition—providing critical data for validating drug targets and screening potential therapeutics. By combining high-throughput screening capabilities with robust analytical methods, we measure key parameters such as reaction rates (kcat), Michaelis constants (Km), and inhibition constants (Ki) to characterize enzyme-substrate and enzyme-inhibitor interactions.
Real-time monitoring of enzymatic reactions using absorbance or fluorescence changes to measure substrate conversion and reaction kinetics.
Automated 96/384-well plate-based assays for rapid screening of compound libraries to identify potential enzyme inhibitors.
Quantitative methods to measure inhibitor potency and characterize binding interactions with target enzymes.
These assays support our antiviral and therapeutic development programs by validating enzyme targets, evaluating lead compounds, and elucidating mechanism-of-action. Our work focuses on viral proteases, host cell enzymes involved in disease pathways, and metabolic enzymes linked to pathological conditions.