Surface plasmon resonance (SPR) is being popular as a technique to monitor a variety of protein-protein interactions. It is considered to be a must to determine the nature of antibody-antigen interactions. The method eliminates the requirement of labeling either of the species that interact and the binding process can be observed in real-time.
SPR provides the data on affinity and concentration however, when properly used, it is able to be able to identify the kinetic parameters of discrete components of the affinity interaction. You can buy an Anti-SPR antibody picoband from Boster bio online.
Many companies present SPR-based, generic antibody screening setups and techniques for speeding the process of determining candidate antibodies with high-quality data panels, and making sure that antibodies with optimal characteristics of kinetic binding are easily recognized.
Surface plasmon resonance (SPR) analysis was used to assess the immunoreactivity of anti-biotin and anti-fluorescein monoclonal antibody after conjugation with the N-hydroxysuccinimide ester of acridinium-9-carboxamide 1. There were only minor changes to their apparent equilibrium dissociation constants of conjugates of antibodies for their ligands occurred as a result of the process of conjugation.
However, a comparison of the initial binding rates of conjugates in combination with their ligands and the antibodies that were not modified over different concentrations indicated that the conjugates for antibodies were in part deactivated. The conjugates that were anti-fluorescein retained at minimum 90% of their immunoreactivity across the modification range examined, while conjugates containing anti-biotin had a decline in the ability to bind with an increase in substitution of the label.