MicroScale Thermophoresis (MST) measures the motion of molecules along microscopic temperature gradients and detects changes in their hydration shell, charge or size.
When performing a MicroScale Thermophoresis (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.
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.
The Monolith systems from NanoTemper provide an easy to use instrument line with minimal moving parts and therefore virtual maintenance free. Depending on the type the dynamic range is between 1 nM (1 pM) – mM and there is also a complete label free instrument. With low sample consumption (16 x 4 µl) per analysis, fast measurements (KD in 10 minutes) and rapid assay optimization, MST is a unique and straightforward platform.
MicroScale Thermophoresis (MST) is an easy, fast and precise way to quantify biomolecular interactions.