Proteases are essential enzymes that cleave peptide bonds and regulate physiological processes including digestion, immune response, and cell signaling. Dysregulated protease activity is associated with cancer, cardiovascular disorders, neurodegenerative diseases, infectious diseases, and inflammatory conditions.
Advances in structural biology, drug design, and screening technologies have expanded the development of protease inhibitors. Accurate measurement of enzyme activity remains essential for identifying and validating selective inhibitors.
Our protease assays use Fluorescence Intensity (FI) technology to measure enzymatic activity. An active protease recognizes and cleaves a defined peptide sequence containing a fluorescent tag. Cleavage separates the fluorescent tag from the peptide substrate and increases the fluorescence signal. The fluorescence intensity therefore reflects the extent of substrate cleavage and protease activity, supporting quantitative inhibitor evaluation.
Activity assays cover serine, cysteine, aspartyl, metalloprotease, aminopeptidase, caspase, coagulation, kallikrein, and viral protease targets.
Panel profiling supports comparison across protease families and evaluation of inhibitor selectivity among related targets.
Reference inhibitors are available for assay validation and comparative characterization of test compounds.
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