Tuesday February 3rd, 2026
Workshop: Monolith X
Cyril Castel, Senior Account Manager Canada from Nanotempertech
Monolith X features the latest innovations for measuring binding affinities: MicroScale Thermophoresis (MST) and Spectral Shift (SpS) technologies. Those methods are based on well-known phenomenon where organic fluorophores report changes in their chemical microenvironment by slight modifications of their emission spectrum, e.g., changes in their overall fluorescence intensity or blue- or red-wavelength shifts. Monolith X exploits this phenomenon by performing ratiometric measurements at two distinct emission wavelengths of a labeled target molecule in the presence of various concentrations of an unlabeled ligand to derive the affinity constant (Kd) for the interaction. The instrument allows for a way to resolve even sub-nanometer spectral shifts, making this approach highly sensitive towards ligand binding events — independent of conformational changes or changes in mass and size upon binding. Moreover, SpS is highly robust against sample impurities and aggregates and provides high quality data with minimal assay development time.
For almost twenty years, NanoTemper Technologies has built products for straightforward interaction analysis known for their ease of use and broad applicability. With the development of SpS technology, scientists have access to a completely new way of measuring molecular binding events that will allow them to characterize even the most challenging interactions successfully.
Wednesday February 18th, 2026
Biophysical affinity-measurement technique, ACTIS (Accurate Constant via Transient Incomplete Separation
Lecture — Tong Ye Wang (Krylov Lab, Postdoc)
Experimental demonstration — Zhiyuan Mao (Krylov Lab, MSc student)
Abstract: Accurate and reproducible measurements of biomolecular binding affinity are essential in both fundamental studies and screening workflows, but many widely used assays can be affected by surface artifacts, labels/tracers, and platform-specific side effects that introduce quantitative bias. This workshop introduces ACTIS (Accurate Constant via Transient Incomplete Separation) — a solution-based method for determining equilibrium dissociation constants (Kd) by resolving free ligand and ligand–target complex under controlled transient incomplete separation and extracting Kd from the resulting separation signatures. The session has two tightly connected components: a lecture covering the theoretical basis of ACTIS and the general experimental workflow, including the key steps from mixture preparation and concentration selection to acquiring separation-based readouts and processing them into binding isotherms and Kd values; and a live demonstration showing the ACTIS instrumental setup and representative runs in real time (sample loading, instrument control, data acquisition, and rapid analysis), with emphasis on practical checkpoints, data-quality indicators, and troubleshooting cues that enable reliable Kd extraction. The workshop concludes with Q&A and an open discussion on how solution-based measurements can strengthen confidence in affinity characterization and inspire new approaches to Kd-determination technology, making it well-suited for researchers in biochemistry, biophysics, analytical chemistry, and drug discovery seeking a hands-on introduction to a robust solution-phase affinity workflow.