For Industry

Finished plasmid DNA, sequencing results confirming cloning success. Bacterial pellets containing the desired protein. Purified protein sample.

Sample quality (aggregation), particle size and molecular weight estimate, ratio of components in the case of mixtures. Offers measurement of the particle size distribution in solution, particle oligomerization, aggregation.

Characterization of affinities of biomolecular interaction. Characterization of affinities and rates of interaction of biomolecules immobilized on the sensor chip with molecules in solution.

Sample characterization by the measurement of their absorbance and fluorescence. Characterization of samples in the infrared spectral region by measuring absorption frequencies of some specific chemical groups (amide bond in proteins).

Determining the secondary structure types in protein: approximate fractions - % of helix, sheet, turns, and random structures.

Identification of proteins in complex mixtures and their relative quantification. Determination of recombinantly expressed or isolated proteins. Characterization of protein modifications. Determination of protein-protein interaction areas and structural changes by hydrogen-deuterium exchange and chemical cross-linking in combination with mass spectrometry.

For the subsequent experimental determination of the 3D structure at atomic level by diffraction analysis, (using the home source or synchrotron). Single crystal X-ray diffraction. Measurement of diffraction data of molecular crystals.

Anti-PSMA antibodies with sub-nanomolar affinity Pre-clinical optimization for developability