Analyzing dissociation kinetics of IgG from protein A
using MP-SPR and PureKinetics™

Application Note #147

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''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:

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Further reading

  • If you are interested in molecular interactions, we recommend to have a look at AN#155 about faster interaction measurements using KineticTitration and AN#138 about interaction of antibody and antigen.

  • 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.

  • Here are a few publications you can have a look at.

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