Affinity determinations of protein interactions using Surface Plasmon Resonance (SPR)

In the recent years there has been a great development in the biosensor area resulting in one of today’s leading technique to measure a wide variety of different types of biological interactions. In a typical experiment the receptor is immobilized on the sensor surface and the ligand is injected over it. The biosensor measure the change of mass over the surface when the ligand binds to the receptor in real time. It is possible to determine kinetics (association and dissociation) and affinity (dissociation constant KD) of the interaction. It is also possible to measure activity and how specific the interaction is. Concentration determinations and epitope mapping are also feasible.

We have a long experience using the Biacore platform and can today offer affinity determination of antibody- antigen interaction. Also other protein- protein interactions or protein-small molecule interactions can be determined.

Please inquire for quotation.

Below are two examples where affinity has been determined of antibody- antigen interactions showing low density (1) and high density (2) interactions.

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