Analyzing dissociation kinetics of IgG from protein A using MP-SPR and PureKinetics™
Application Note #147
The PureKinetics™ sensogram shows the true binding response without bulk artifacts. Using the PureKinetics™ feature, the IgG dissociation in changing buffers could be quantified.
IgG dissociation kinetics from immobilized Protein A was studied using real-time Multi-Parametric Surface Plasmon Resonance (MP-SPR). Various dissociation buffers were tested to determine the most efficient solution. A unique feature, PureKinetics™, allows differentiation of real binding from interfering bulk signal artifacts, providing a pure binding signal. The method can clear out even extremely large bulk signals, such as high-ionic strength dissociation buffers. In this study, the most efficient dissociation from Protein A was achieved with buffers of pH below 4.0.
Recommended instrument for this application
Further reading
- If you are interested in molecular interactions, we recommend to have a look at AN#155 about faster interaction measurements using KineticTitration.
- Do you want to find out how to calculate thickness out of MP-SPR measurements? Click here
- Do you want to see how MP-SPR instruments work? Click here
- Do you want to see MP-SPR instruments comparison? Click here