MST - Instruct-CZ

The Monolith systems measure equilibrium binding constants for a variety of molecules - thus allows to measure wide range of interactions from ion fragment binding up to interactions of large complexes (liposomes and ribosomes). This method allows to detect changes in hydration shell, charge or size of molecules and thus detect biomolecular interaction. Volume of buffer is kept constant in whole dilution series so the observed alterations in the thermophoretic depletion or enrichment can come only from changes in the size, charge or solvation entropy of the Auorescently labeled molecule caused by binding of non-labeled molecule to the labeled one.

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MST - Instruct-CZ

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User Guide

Microscale Thermophoresis (MST)

The Monolith NT.115 MST device allows to detect changes in hydration shell, charge or size of molecules and thus to detect biomolecular interactions.


MST can be used for:

  • Determination using a fluorescent dye or fluorescent protein of the affinity of interaction from 1nM to mM.


Sample requirements:

  • Concentration of fluorescent labeled molecule: 10 nM - 10 mM;
  • Final concentration of unlabeled molecule should be at least two orders of magnitude above the expected Kd value. To perform simulations of binding events and to help choose the appropriate concentration, the “Concentration Finder” software is available on the device control panel;
  • At least 20 µl samples per capillary is needed.