Phosphodiesterases (PDEs) regulate intracellular levels of cyclic nucleotides such as cAMP and cGMP by catalyzing their hydrolysis. Dysregulated PDE activity is associated with erectile dysfunction, pulmonary hypertension, neurodegenerative disorders, and other diseases.
Selective inhibition of individual PDE isoforms enables modulation of cyclic-nucleotide signaling and provides a foundation for therapeutic development across diverse disease areas.
PDE hydrolytic activity is measured by monitoring the breakdown of dye-labeled cyclic nucleotides. PDE-mediated hydrolysis exposes the resulting nucleotide monophosphate, allowing high-affinity beads to bind the product. This interaction changes the motion of the fluorescent molecular complex and generates a measurable fluorescence-polarization (FP) signal. The degree of cyclic-nucleotide hydrolysis reflects PDE activity and supports evaluation of small-molecule inhibitor potency.
Activity assays are available across a broad range of PDE families and isoforms.
Cross-family and within-subtype profiling supports assessment of inhibitor selectivity, including comparisons across PDE4 targets.
Reference compounds are available for target-specific assay validation and comparative inhibitor characterization.
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