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Microscale Thermophoresis analysis enables to study biomolecular interactions without prior purification or immobilization of the interactors. It gives access to the determination of the binding properties in terms of affinity (in the range from 10-2 to 10-11 M) and stoichiometry. The principle of the method takes into account the motion of molecules along microscopic temperature gradients and detects changes depending on their free or bound states. These changes are detected and quantified by measuring changes in fluorescence associated to one of the interactors.