usage
sufficient for 100 fluorometric tests
detection method
fluorometric
storage temp.
−20°C
General description
Trypsin (EC3.4.21.4) is a digestive, serine protease that hydrolyzes dietary proteins in many eukaryotic and prokaryotic organisms. Trypsin predominantly cleaves peptide chains at the carboxyl side of lysine and arginine amino acids, but not before proline.
Application
Suitable for evaluation of drugs and screening of potential inhibitors to trypsin proteases.
Biochem/physiol Actions
The Trypsin Inhibitor Assay Kit uses a fluorescein isothiocyanate (FITC)-labeled synthetic substrate. The fluorescein label is highly quenched. Upon digestion by trypsin present in the sample, the substrate is cleaved into smaller peptides, which abolishes the quenching of the fluorescence label. The fluorescence or fluorescence polarization (FP) of the FITC-labeled fragments is measured at λex/em = 485/530 nm. Inhibition is determined by the decrease in fluorescence.
存储类别
10 - Combustible liquids
怎么回事?
WGK 1