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

Application Note #147

AN_147.png

Figure 2. 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:

200_otso_small.jpg 400_KONTIO_LOGO_24012019_cropped.jpg 210_vasa_small.jpg 410A_KAURIS_instrument.jpg  220A_naali_small.jpg 420_ilves_small.jpg
200 OTSO 400 KONTIO 210A VASA  410A KAURIS  220A NAALI 420A ILVES 
green-tick.png   green-tick.png green-tick.png  green-tick.png  green-tick.png green-tick.png 

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.

DOWNLOAD APPLICATION NOTE IN PDF


Back to all Application Notes