Biolayer Interferometry

Content tagged with Biolayer Interferometry

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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 kinetic binding assay using Surface Plasmon Resonance (SPR) or Biolayer Interferometry (BLI), how do I chose which of my binding partners to immobilize?

FAQ

The relative size of the molecules isn't generally the deciding factor. Large proteins will typically give larger signals, but that isn’t necessarily better.

For protein/protein interactions, start by considering other properties of the proteins. Most...

Biolayer Interferometry (BLI)

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The Octet RED384 and BLItz instruments from Sartorius detect Biolayer Interferometry, an optical technique used to measure binding kinetics and binding equilibrium.