Binding kinetics

The accurate measurement of binding kinetics between two biomolecular entities is an essential step in assay development. Biomolecular affinity measurement is typically described by a constant, named KD (affinity constant or equilibrium dissociation constant). This KD is a measure of the equilibrium concentration at which half of the molecules are bound. It is calculated by dividing the rate of dissociation by the rate of association.

Existing technologies, such as SPR and BLI have limitations affecting the accuracy of the resulting data. To circumvent these problems, we use the iRiS Kinetics MX-100 system for the measurement of binding kinetics.

For example, iRiS Kinetics technology is very stable and allows for very long measurements. It is therefore possible to measure very long dissociation rates directly.

To request a quote, please fill out the information in this form. The cost to measure the binding affinity of one pair of biomolecules is priced at $950. Discounts are available for higher number of measurements. For example, multiple antibodies can be immobilized and relative binding of an antigen measured in the same experiment.