Studying the binding affinity of different ERK2 binding partners with MicroScale Thermophoresis
ERK2 is an important player in multiple biochemical signaling pathways and is involved in different cancer types. This highly relevant pharmaceutical target represents an optimal model system to demonstrate the capabilities of our MicroScale Thermophoresis (MST) platform.
In this example study, the binding affinity of ERK2 (MAPK1, mitogen-activated protein kinase 1) towards the following four different binding partners (size range from 0.3 kDa to 150 kDa) was studied by MST:
• ERK2 Inhibitor I (Merck)
• ERK2 Activation Inhibitor Peptide I (Merck)
• Aptamer C5.71 (Mayer lab, Bonn)
• Antibody 1B3B9 (Merck)
The results (figure to the right) demonstrate that our MST platform is perfectly suited to study molecular interactions independent of the size and mass of the ligand. Therefore, MicroScale Thermophoresis is the optimal tool to characterize drug-target, antibody-antigen or aptamer-target interactions in terms of basic binding parameters.