Products

Data file

28-9782-62

MicroCal iTC Systems

Application notes

28-9870-38         
Revealing Kinase Inhibitor Mechanisms

28-9870-43       
The use of ITC for obtaining enzyme kinetic constants

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Studying low-affinity fragments of ligands by ITC

Isothermal Titration Calorimetry (ITC)

Isothermal Titration Calorimetry (ITC) is the gold standard for measuring biomolecular interactions.  ITC simultaneously determines all binding parameters (n, K, ΔH and ΔS) in a single experiment – information that cannot be obtained from any other method.

When substances bind, heat is either generated or absorbed.  ITC is a thermodynamic technique that directly measures the heat released or absorbed during a biomolecular binding event.  Measurement of this heat allows accurate determination of binding constants (K_B), reaction stoichiometry (n), enthalpy (ΔH) and entropy (ΔS), thereby providing a complete thermodynamic profile of the molecular interaction in a single experiment.  Because ITC goes beyond binding affinities and can elucidate the mechanism of the molecular interaction, it has become the method of choice for characterizing biomolecular interactions.

Products

MicroCal offers a range of ultrasensitive isothermal titration calorimeters, including the industry standard VP-ITC and the new iTC₂₀₀ and Auto-iTC₂₀₀ with their reduced sample requirements and higher throughput.

Need more information? Contact us.

Journal Citations for iTC₂₀₀ and Auto-iTC₂₀₀