Enabling better drug discovery decisions through chemical proteomics.

Generate quantitative target engagement and selectivity data to prioritize the right candidate with confidence.

Why chemical proteomics?

Native biological systems

Measure target engagement directly in living cells and other native biological systems rather than relying on simplified biochemical assays.

Endogenous protein profiling

Profile target engagement and selectivity across hundreds of endogenous proteins simultaneously, revealing both intended and unexpected interactions.

Cross-model profiling

Apply the same quantitative chemical proteomics workflows across cell lines, in vivo models, and PBMCs to directly compare target engagement as compounds progress through drug discovery.

Where you measure matters just as much as what you measure.

Whether you are developing kinase inhibitors, serine hydrolase inhibitors or covalent drugs, we wouldd be happy to discuss the most appropriate chemical proteomics strategy.

Kinase inhibitor profiling – CellEKT®

Quantitatively profile target engagement and selectivity across up to 90% of endogenous kinases in biologically native systems.

Serine hydrolase inhibitor & activity-based protein profiling

Measure target engagement and selectivity of serine hydrolase inhibitors by using proteomics- and gel-based activity-based protein profiling (ABPP).

Covalent inhibitor profiling

Profile covalent inhibitors using residue specific probes or  tailored probes, enabling measurement of target engagement across endogenous proteins.

Ensure every development decision is guided by biology that actually matters.

Joel Rüegger, CEO

Activity-based protein profiling & serine hydrolases

Activity-based protein profiling & serine hydrolases

Activity-based Protein Profiling was first introduced in 1999 in a seminal paper by the group of Benjamin Cravatt. The idea is beautiful in its simplicity: turn covalent inhibitors (sometimes called ‘suicide substrates’) into a ‘probe’, a molecule that can be...