MP-SPR is a sensitive platform to determine antibody and fragment binding on antigen. Label-free interactions are measured in real-time, revealing affinity and kinetics of the binding. MP-SPR instruments can also handle target molecules incorporated in liposomes (membrane extract) and living cells enabling interaction measurements in natural-like environment.
Interaction measurements can be performed in diverse fluids including 100% serum, plasma or cell growth medium. With PureKinetics™, bulk effect can be distinguished from binding and thus high precision results are obtained. MP-SPR with LayerSolver™ provides insight into the conformation and orientation of the antibodies.
"MP-SPR is a flexible instrument that allows us to connect the power of traditional separation techniques, such as LC, with the quantification of interactions by SPR. This way, we are able to separate the analytes prior to specific, label-free, real-time analysis of their biochemical interaction on a sensor chip. For instance, interactions of individual components of antibody preparations can be studied using immobilized antigen on the SPR surface." Asst. Prof. Jeroen Kool, VU Amsterdam, The Netherlands
MP-SPR Navi™ Regenerable avidin kit is an excellent tool in development of
MP-SPR based assays. The kit allows the user to conduct precise and highquality
measurements in shorter time and convenient experimental set-up.
Besides having the ligand available with biotin-conjugation, one does not
need to optimize buffers and immobilization conditions. Finally, the costeffectiveness
of SPR measurements improves since the same sensor slide
can be completely regenerated up to 100 times.
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MP-SPR Navi™ Regenerable avidin kit is an excellent tool in development of MP-SPR based assays. Here, the specific binding affinity of lipid based molecules towards sensor-captured protein was analyzed. Also, concentration analysis of diagnostically relevant biomarkers were performed in human serum samples. Utilizing Regenerable avidin kit reduces time in assa development since there is no need to do traditional immobilization conditions optimization which is typically needed for covalent immobilization over dextran sensor slides.
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Figure 3. Anti-HSA binding to the immobilized HSA with four different concentration. Injection is started at time point zero and arrow is showing ending point. Calculated binding constants for the interaction is presented in the table.
Human serum albumin antibody (anti-HSA) interaction with immobilized human serum albumin (HSA) was measured using Multi-Parametric Surface Plasmon Resonance (MP-SPR). As assumed, commercial anti-HSA binds strongly to the HSA and dissociates extremely slowly from the HSA. Steady state binding as well as kinetic of the binding was calculated for the interaction.
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