Microscale Thermophoresis is a powerful method to quantify biomolecular interactions. It measures the motion of molecules along microscopic temperature gradients and detects changes in their hydration shell, charge or size. By combining the precision of fluorescence detection with the flexibility and sensitivity of thermophoresis, MST provides a flexible, robust and fast way to measure molecular interactions.When performing a MST experiment, a microscopic temperature gradient is induced by an infrared laser, and the directed movement of molecules is detected and quantified using either covalently attached dyes, fluorescent fusion proteins or intrinsic tryptophan fluorescence. The applications range from small-molecule binding events to protein-protein interactions and interactions of multi-protein complexes. (www.nanotemper.com).This technique is applied to quantify biomolecular interactions from ions and small molecules to high molecular and multi-protein complexes and, also, bulky assemblies such as liposomes and nanodiscs.
Our Monolith instrument use capillary format and, for each experiment it is necessary to have a constant concentration of a fluorescent probed molecule (e.g. labelled protein) and variable concentration of any tittrant (eg. other protein, ligands, etc). To perform one simple curve in this device it is necessary only 4ul of sample per capillary.
The LEC Monolith device is out of users portal, for more information about how to use this device and sample preparation, please contact our staff. The LEC does not provide any kind of consumables for this device.