
Microcal Isothermal Titration Calorimetry (ITC) 200
MicroCal ITC 200
Isothermal Titration Calorimetry (ITC) is the gold standard for measuring biomolecular interactions. ITC simultaneously determines all binding parameters (n, K, âH and ÎS) in a single experiment â 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), reaction stoichiometry (n), enthalpy (âH) and entropy (ÎS), 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.
Capabilities
- âCharacterization of molecular interactions of small molecules, proteins, antibodies, nucleic acids, lipids and other biomolecules.
- âLead optimization.
- âEnzyme kinetics.
- âAssessment of the effect of molecular structure changes on binding mechanisms.
- âAssessment of biological activity.
- âProtein-small molecule
- âProtein-protein
- âTarget-drug
- âEnzyme-inhibitor
- âAntibody-antigen
- âProtein-DNA
- âProtein-lipid
- âSmall molecule-small molecule
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