Surface plasmon resonance (SPR) is currently popular as a technique to study a wide range of protein-protein interactions. SPR is considered to be a standard to determine the nature of antibody-antigen interactions. The method eliminates the requirement to label one or both of the two species in question and the binding process can be observed in real-time. 

Therefore, it is well to screen for non-purified, crude antibody samples which dominate early panel candidates following the antibody selection campaign. SPR yields the data on affinity and concentration however, if used properly, it can also reveal the kinetic parameters of discrete components of the affinity interaction. You can know more about an SPR antibody via www.bosterbio.com/anti-spr-picoband-trade-antibody-a00416-1-boster.html.

In this article, we present SPR-based general antibody screening configurations and techniques for speeding the process of determining candidate antibodies with high-quality data panels and making sure that antibodies with optimal binding characteristics for kinetics are easily recognized.

Surface plasmon resonance (SPR) can be utilized to study binding affinity and kinetic parameters that exist between the analyte and a ligand. SPR is possible to perform by either cross-linking a ligand to a sensor chip covalently or using non-covalent interactions with high affinity to secure the ligand to a certain configuration to a chip both of which offer advantages. 

SPR measurements are based on mass and reveal the proportion of the analyte that is bound to a particular chemical ligand at a certain concentration when it is flowed at a predetermined speed to determine how binding occurs in the biochemical interaction.