Malvern MicroCal iTC200 for understanding biomolecular interactions using ITC

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Isothermal titration calorimetry (ITC) enables label-free measurement of binding events by measuring the heat released or absorbed during biochemical binding. Binding affinity (KD), stoichiometry (n), enthalpy (ΔH) and entropy (ΔS) can all be measured to provide deeper insights into structure-function relationships and the mechanisms of binding.

Requiring no assay development, the MicroCal iTC200 provides results quickly and is a suitable tool for any research laboratory studying biomolecular interactions. High sensitivity, using as little as 10 μg of protein, provides good signal-to-noise to generate high-quality data over a wide range of affinities, from weak to tight binders. Integrated with user-friendly software, operators are guided for fast and accurate analysis. A baseline-fitting algorithm eliminates the need for tedious post-run manual manipulation.

Applications range from drug discovery and design for characterising biomolecular interactions to fundamental research such as the understanding and regulation of signal transduction pathways. The types of interactions that can be studied are not limited to proteins and there are numerous references in the literature where ITC has been used to understand how nucleic acids and lipids, as well as proteins, function in biological systems.

The product features no labelling, no immobilisation and no molecular weight limitations. It can measure millimolar to nanomolar affinities and nanomolar to picomolar disassociation constants. It is upgradeable to the fully automated MicroCal Auto-iTC200 system.