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VLP binding was monitored in situ by QCM-D after formation of the bilayers on a SiO2 coated sensor and blocking with BSA.
Finally they were washed thrice in PBS, fixed in paraformaldehyde (1%) and the binding was monitored in a flow cytometer (FACSCalibur, Becton Dickinson, San Jose, CA).
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PAPS binding was monitored via binding-induced changes in the intrinsic fluorescence of SULT1A1.
Binding was monitored by the colorimetric conversion of nitrocerfin by a β-lactamase fusion to DCC.
The protein binding was monitored by FET and direct current (dc) measurements.
Nonspecific binding was monitored using IgM as control sample.
Plasminogen, immobilized to beads, was used as a capturing tool for PrPSc in brain homogenates from scrapie affected sheep and the binding reaction was monitored in real-time in an ultrasonic cell.
The binding is monitored by following the change in the square wave voltammetry (SWV) reduction peak signal of ferrocyanide/ferricyanide redox couple due to the removal of the negatively charged aptamers from the surface upon protein binding.
Competitive binding to VEGF between VEGFR and bevacizumab was monitored in real-time.
Competitive binding to VEGF between VEGFR and bevacizumab was monitored in real-time using this platform.
Subsequently, the binding of His6-GFP to these surfaces and its release upon UV-irradiation was monitored in real time with QCM.
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