Isothermal Titration Calorimetry (ITC) is a biophysical technique for directly measuring the thermodynamics of molecular interactions. By monitoring the heat released or absorbed during a binding event, ITC provides a comprehensive profile of the interaction, including binding affinity (Kd), stoichiometry (n), enthalpy (ΔH), and entropy (ΔS). This label-free and solution-based method is ideal for studying a wide range of biomolecular interactions, such as protein-ligand, protein-protein, and nucleic acid interactions. ITC enables detailed characterization of binding mechanisms, making it an invaluable tool for drug discovery, lead optimization, and biomolecular research.
In an ITC assay, a solution containing the ligand is gradually titrated into a solution containing the target molecule under isothermal (constant temperature) conditions. The heat released or absorbed during each binding event is measured with high sensitivity, allowing for the calculation of key thermodynamic parameters, including binding affinity (Kd), stoichiometry (n), enthalpy (ΔH), and entropy (ΔS).
In-House Proteins: Our highly active, in-house produced proteins enable a wide range of biophysical assays, ensuring high precision, reliability, and reproducibility.
Versatile Applications: Designed for direct binding studies, competitive binding assays, and thermodynamic analyses, including enthalpy and entropy profiling, providing a robust platform for understanding molecular interactions.
Broad Range of Biomolecules: Ideal for studying a variety of biomolecular interactions, including protein-protein, protein-small molecule, and enzyme-ligand interactions. Applications include drug screening, lead optimization, enzyme kinetics, and other research areas requiring detailed interaction analysis.
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