Related Experiment Video
Updated: May 13, 2026
Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
Published on: April 17, 2017
Capture of the human IgG1 antibodies by protein A for the kinetic study of h-IgG/FcγR interaction using SPR-based
1Physico-Chemistry Department, Centre d'Immunologie Pierre-Fabre, Saint Julien-en-Genevois, France.
Surface plasmon resonance (SPR) is a key technology to evaluate IgG effector functions in vitro involving binding to Fcgamma receptors (FcγR). We describe here the chemical coupling of protein A to a sensor chip. IgGs prepared either from purified antibodies or from crude cell media supernatants are captured by the protein A and are used as the ligand. Soluble forms of FcγRs are injected at different concentrations and are used as the analyte. This setup allows the definition of the kinetic rates of binding of the FcγRI (high affinity) or the FcγRIIIa (low affinity) on the Fc domain of IgGs.
Surface plasmon resonance (SPR) is a key technology to evaluate IgG effector functions in vitro involving binding to Fcgamma receptors (FcγR). We describe here the chemical coupling of protein A to a sensor chip. IgGs prepared either from purified antibodies or from crude cell media supernatants are captured by the protein A and are used as the ligand. Soluble forms of FcγRs are injected at different concentrations and are used as the analyte. This setup allows the definition of the kinetic rates of binding of the FcγRI (high affinity) or the FcγRIIIa (low affinity) on the Fc domain of IgGs.
More Related Videos
10:33Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
08:58Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
