Spectrophotometry and luminescence
Description: Sample characterization by the measurement of their absorbance and fluorescence. Allows studying enzyme activity, interaction with ligands (by the measurement of fluorescence polarization), FRET, ELISA, to determine protein and DNA concentrations. Can be measured in cuvettes and plates.
Input: Min.100 μl of biomolecule solution.
Output: Spectra, kinetics and its analysis.
Time: Up to one week
Approximate price: in request
Fourier Transform Infrared Spectroscopy
Description: Characterization of samples in the infrared spectral region by measuring absorption frequencies of some specific chemical groups (amide bond in proteins). It allows to determine protein secondary structure, interaction with ligand and structural changes.
Input: Min. 30 μl biomolecule solution at concentration 3-5 mg/ml.
Output: FTIR spectrum and its characterization. Information on the secondary structure and the interaction of the molecule with the ligand.
Time: One week
Approximate price: on request