SPR vs ITC vs MST vs BLI: Discover your optimal interaction technique with our Comparison & Quiz

SPR vs ITC vs MST vs BLI: Discover your optimal interaction technique with our Comparison & Quiz

Protein-protein interactions were analyzed on OpenSPR™, Biacore™ and IBIS™ instruments Kinetic analysis was used to determine the on rate, off rate, and affinity constant of the interaction of 2 different ligands with an analyte All three instruments produced acceptable kinetic constants within the expected error range for these experiments, validating the OpenSPR™ instrument against other commercial SPR equipment OpenSPR is a benchtop surface plasmon resonance (SPR) solution which provides researchers with the ability to complete in-depth label-free binding kinetics in their own lab. When searching for an SPR solution, researchers have to choose from various performing tools for different applications. Addressing the performance of the tools and establishing their consistency and accuracy is important when making a purchasing decision. We always get asked about when we will create a comparison study between our OpenSPR and other more expensive commonly used tools and so we are responding with this great comparison study. In this study, we will investigate the binding kinetic results of protein-protein interactions and how they compare between OpenSPR, Biacore T100 and IBIS MX96 SPR systems.

What Binding Kinetics Can Tell You That Affinity Can’t

What Binding Kinetics Can Tell You That Affinity Can’t

There are many techniques available that can provide scientists with the affinity of an interaction between two biomolecules. The affinity describes how strong the interaction is between two biomolecules. Extremely strong interactions can be on the order of picomolar affinities, while weak interactions can be in the millimolar range, with many interactions falling within this range. Mathematically, the affinity is the concentration of analyte at which half of all binding sites are occupied (at equilibrium conditions).

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