MicroScale Thermophoresis

Content tagged with MicroScale Thermophoresis

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Measuring Molecular Interactions

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A wide array of biomolecular interactions from protein/protein interactions to small molecule ligand/compound binding interactions are important in biology. Fundamentally, there are two ways to measure (or quantify) binding of any of these interactions...

I want to measure a Kd, how do I choose which technique is best?

FAQ

The CMI has four primary technologies to quantify molecular interactions: Surface Plasmon Resonance (SPR) and Biolayer Interferometry (BLI), Isothermal Titration Calorimetry (ITC) and MicroScale Thermophoresis (MST). Each technologies has its advantages...

To measure a molecular interaction, how do you choose which molecule to be kept at a fixed concentration and which to vary in concentration?

FAQ

The choice of which molecule to keep constant and which to vary will depend on the experiment type, the properties of the molecules and the stoichiometry of the interaction.

For ITC, where neither protein is labeled or immobilized, either molecule can be...

For a binding assay using MicroScale Thermophoresis (MST), which binding partner should be fluorescently labeled?

FAQ

MST experiments on the Monolith NT.115 pico require that one of the binding partners is fluorescently labeled.

For protein/protein interactions, start by considering the amounts, solubility and sequence of the proteins. The labeled target is typically...

MicroScale Thermophoresis (MST)

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The Monolith NT.115pico from NanoTemper detects MicroScale Thermophoresis, movement in a temperature gradient, used to measure binding equilibrium.