Surface plasmon resonance (SPR) is used to monitor biomolecular binding events in real time.This is a high performance research system available for label-free studies of biomolecular binding.
Isothermal titration calorimeter (ITC) system directly measures the heat released or absorbed during a biomolecular binding event. The result is a direct, label-free measurement of binding affinity and thermodynamics in a single experiment. The applications of ITC range from drug design, protein-protein, protein-membrane and more.
The VP-DSC is a differential scanning microcalorimeter. The DSC is a highly sensitive technology for studying moleculs in solution. It is used to measure the stability of structured micromolecules such as proteins and nucleic acids.
The MST is a powerful tool that enables characterization of the thermal stability of proteins and other biomolecules. It is a simple method that delivers the ‘Gold Standard’ in TM biosimilarity and batch-to-batch comparability assessment, as well as for the optimization of purification and manufacturing conditions. Our DSC system is simple to use, requiring little assay development, and no labelling or immobilization.
Nanosight is used for rapid, automated analysis of size distribution and concentration of all types of nanoparticles ranging from ~10nm to 1000nm in diameter. Fluorescent particles can be measured with four lasers.
Microscale thermophoresis (MST) is the directed movement of particles in a microscopic temperature gradient. MST is a rapid and precise method to quantify biomolecular interactions in solution at micromolar scales.
Field-flow fractionation (FFF) can separate quantitatively particles over a wide size range. A field is applied to a suspension or solution pumped through a long and narrow channel, perpendicular to the direction of flow. The results in separation of the particles present in the fluid, depending on their differing mobilities under the force exerted by the field.
nanoDSF (Differential Scanning Fluorimetry ) is a method for easy, rapid and accurate analysis of protein stability and aggregation. DSF detects changes in the fluorescence of tryptophan and tyrosine in the protein. The fluorescence of tryptophans and tyrosines in a protein is strongly dependent on their close surroundings. Since no secondary reporter fluorophores are required, protein solutions can be analyzed independent of buffer compositions, and over a concentration range of 250 mg/ml down to 10 µg/ml. This allows for the analysis of detergent-solubilized membrane proteins, as well as for highly concentrated antibody formulations.