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Beckman Coulter ProteomeLab XL-I analytical ultracentrifuge is equipped with absorbance (wavelength range 190 – 800 nm) and interference optics and can be used for both sedimentation velocity and sedimentation equilibrium experiments. Analytical ultracentrifugation is applicable for proteins, nucleic acids, lipids, polysaccharides, viruses and nanoparticles. It has a broad applicability including determination of sample homogeneity, oligomeric state of proteins (or molecular weight, respectively) and can be used to assess aggregation of sample and to study biomolecular interactions of self- and hetero-association systems (determination of stoichiometry and affinity).
Fully automated isothermal calorimeter AutoITC200 with ultrasmall working cell (200 µl). ITC method is used for characterization of biomolecular interactions of small molecules, proteins, antibodies, nucleic acids, lipids and others. Enzyme kinetics, biological activity or the effect of molecular structure changes on binding mechanism can be also assessed. Complete thermodynamic profile of the molecular interaction in a single experiment (stoichiometry, Ka, ∆H and ∆S values).
VP-ITC is isothermal calorimeter with 1400 µl volume of working cell. ITC method is used for characterization of biomolecular interactions of small molecules, proteins, antibodies, nucleic acids, lipids and others. Complete thermodynamic profile of the molecular interaction can be obtained in a single experiment (stoichiometry, Ka, ∆H and ∆S).
PEAQ-DSC is differential scanning microcalorimeter with <200 µl volume of sample capillaries. DSC technique measures the heat changes that occur in the (bio)molecule sample solution during a controlled increase or decrease in temperature, on the basis of a temperature difference between the sample and the reference material. Automated version of PEAQ-DSC enables to run up to 282 samples in a row unattended.
VP-DSC is differential scanning microcalorimeter with 500µl volume of sample cell. DSC technique measures heat changes that occur in the (bio)molecule sample solution during a controlled increase or decrease in temperature, on the basis of a temperature difference between the sample and the reference material.
The Monolith systems measure equilibrium binding constants for a variety of molecules – thus allows to measure wide range of interactions from ion fragment binding up to interactions of large complexes (liposomes and ribosomes). Monolith NT.115 Pico allows analysis of high-affinity interactions down to pM range.
Biosensor system Octet utilizes BLI technology (biolayer interferometry) to detect the interaction parameters (kinetics, affinity) on a sensor chip. Octet RED96e enables simultaneous measurement of 8 channels ensuring high throughput. System is suitable especially for protein-protein or protein-nucleic acid interactions, however other binding systems can be evaluated as well.
Biacore S200 is a successor of T200 model with higher sensitivity. This system monitors real-time, label-free interactions ranging from ions to viruses. The system offers a powerful, versatile solution for obtaining the highest quality kinetic, affinity, concentration, specificity, selectivity, and thermodynamic data and can be used for multiple applications, from early research to drug discovery and development. In the arrangement, one of the interactants is immobilized on the sensor chip surface, while the other is passed over that surface in solution.
Analytical size-exclusion chromatography coupled to an array of detectors including UV-VIS spectrometer, refractometer, viscometer and static light scattering (RALS/LALS). Suitable for analysis of sample purity, oligomeric state of proteins, study of complexes and other experiments.
Dynamic light scattering is used for the analysis of protein solutions, aggregates, promiscuous inhibitors, buffers, nanoparticles, polymers or other products in solution. DLS system measures the polydispersity of the sample and hydrodynamic radii (size) of the particles within range of 0.4 to 5,000 nm. This is particularly beneficial in sample characterization prior to crystallization or other experiments.
Dynamic light scattering is used for the analysis of protein solutions, aggregates, promiscuous inhibitors, buffers, nanoparticles, polymers or other products in solution. SpectroLight 600 can measure samples in plate fromat in submicroliter droplets. This enables direct detection of particles in crystallization plates.
Automated high throughput protein crystal drop imaging system provides ultraviolet and visible crystal imaging and protein crystal monitoring that automatically image crystallization experiments and link images with crystallization conditions. Automated system contains fully integrated system for temperature controlled incubation, inspection, and analysis of protein crystallization plates.
Microdeposition system for biosensor arrays
The sciFLEXARRAYER S1 is a compact automated non-contact dispensing system of ultra-low volumes. It consist of piezo dispensing unit and precision equipment for liquid handling.
UV-VIS spectrophotometer: Biospectrometer kinetic
Spectrophotometer allows measurement of samples in range of 200-830 nm. Can be used to determine protein or nucleic acid concentration, purity and also to measure basic enzyme kinetics.