
The BIACORE T200 is a versatile, high-performance Surface Plasmon Resonance (SPR) system for detailed, label-free, real-time analysis of biomolecular interactions. It delivers high-quality kinetic, affinity, concentration, specificity, selectivity, comparability, and thermodynamic interaction data with exceptional sensitivity. Technical specifications include the ability to monitor almost any molecular interaction where one partner can be immobilized on a sensor surface. It supports the use of 96- and 384-well microplates and vials, enabling analysis of up to 384 samples in unattended runs. The system features four flow cells, allowing for simultaneous monitoring of interactions. It offers a wide kinetic range, measuring association rate constants (ka) from 10^3 to 10^7 M^-1s^-1 and dissociation rate constants (kd) from 10^-5 to 0.5 s^-1. The analysis temperature range spans from 4°C to 45°C, with temperature control for sensitive samples. Applications include increasing understanding of molecular mechanisms, defining potential drug targets, selecting and characterizing biotherapeutic candidates, and optimizing lead compounds during drug discovery. It is widely used for protein-protein and protein-small molecule interaction studies, antibody characterization, and mechanistic studies of biomolecular interactions. The system's high sensitivity allows for precise affinity analysis of small organic compounds and detection of low abundance proteins. The BIACORE T200 features wizard-supported software for assay development, analysis, data evaluation, and interpretation, making it user-friendly. It also includes a built-in buffer selector for up to four different buffers in a single run and the capability for sample recovery for identification by mass spectrometry.

Faculty of Medicine and Health Sciences
Research lab focused on advancing scientific knowledge and innovation.
The BIACORE T200 is a versatile, high-performance Surface Plasmon Resonance (SPR) system for detailed, label-free, real-time analysis of biomolecular interactions. It delivers high-quality kinetic, affinity, concentration, specificity, selectivity, comparability, and thermodynamic interaction data with exceptional sensitivity. Technical specifications include the ability to monitor almost any molecular interaction where one partner can be immobilized on a sensor surface. It supports the use of 96- and 384-well microplates and vials, enabling analysis of up to 384 samples in unattended runs. The system features four flow cells, allowing for simultaneous monitoring of interactions. It offers a wide kinetic range, measuring association rate constants (ka) from 10^3 to 10^7 M^-1s^-1 and dissociation rate constants (kd) from 10^-5 to 0.5 s^-1. The analysis temperature range spans from 4°C to 45°C, with temperature control for sensitive samples. Applications include increasing understanding of molecular mechanisms, defining potential drug targets, selecting and characterizing biotherapeutic candidates, and optimizing lead compounds during drug discovery. It is widely used for protein-protein and protein-small molecule interaction studies, antibody characterization, and mechanistic studies of biomolecular interactions. The system's high sensitivity allows for precise affinity analysis of small organic compounds and detection of low abundance proteins. The BIACORE T200 features wizard-supported software for assay development, analysis, data evaluation, and interpretation, making it user-friendly. It also includes a built-in buffer selector for up to four different buffers in a single run and the capability for sample recovery for identification by mass spectrometry.


Faculty of Medicine and Health Sciences
Research lab focused on advancing scientific knowledge and innovation.
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