Biomolecular Interaction Laboratory

	How  much, fast, and strong is the binding of  an analyte to its ligand? IBIS MX96 has increased sensitivity, which allows kinetic analysis at very low ligand densities for reduction of rebinding effects. This is essential for calculating the apparent affinity constant of the biomolecular interaction pair. Concentration measurements can be performed at high speed using the mass transport limitation (MTL) effect. Because of unlimited exposure times high affinity interactions can be measured at very low concentrations upto a picoMolar (IgG).
	How can the overlap be screened of antibodies that bind to various epitopes?  Clustering of antibodies using the IBIS MX96/CFM combination is very time and cost effective. Competing and non-competing antibodies are determined in parallel and in a single measurement a line of the competition map (checkerboard) is measured at once. Additionally crude supernatants at low concentrations can be used for antibody clustering/binning.
	How can patients with complex diseases be monitored? 1) Disease monitoring that give profound better outcome for patient treatment, when multi-analytes are detected and correlated. 2) Diseases with high variability between patients including interfering diseases 3) Diseases for monitoring the effect of therapy. (Theranostics). 4) Early diagnosing of pathway failures in systems biology
	How can an analyte be captured and eluted from its ligand? The microarray area allows capturing of ligand using the affinity chromatography principle. The captured analyte can be eluted from the sensor chip and used for Mass Spectrometry (MS) analysis.