Surface plasmon resonance (SPR) is currently extensively used as a method to monitor a variety of protein-protein interactions. SPR is considered to be the standard to determine the nature of the interactions between antibodies and antigens. This technique eliminates the requirement of labeling either of the two species in question and the binding process can be observed in real-time. 

Therefore, it is well suitable for the screening of non-purified, crude antibody samples that are the most prevalent panel candidates following the antibody selection campaign. You can visit the site www.bosterbio.com/anti-spr-picoband-trade-antibody-a00416-1-boster.html to know about SPR antibody kits. 

SPR yields both affinity and concentration data; however, when properly used, it is able to identify the kinetic parameters of discrete components of the affinity interaction. Surface plasmon is an optic process used to detect molecular interactions.

The binding of a mobile molecule (analyte) to an immobilized molecule on a thin film of metal (ligand) alters its refractive index. Light's angle of extinction reflecting after polarized light is impinging on the film, is changed, and monitored by changing the detector position to detect the dip in the intensity of reflection.

Since the method is only able to detect mass and not mass, there is no requirement to label the interconnected components and thus avoiding any possible alteration in their molecular properties. We have used surface resonance to study the interaction between hair cells' proteins.