Macromolecular protein complexes are known to have key regulatory roles that are linked to most biological processes. Maximizing expression, efficient purification and deciphering the functional role of complexes and their components are main objectives for researchers working with proteins. Of equal importance but often overlooked is monitoring the quality of a protein preparation particularly as it relates to the protein’s functionality. By having more insights into the quality of a protein sample, researchers can be more succesful and efficient in their experimental setup and planning. The Tycho NT.6 system quickly analyzes protein samples and provides detailed information on their folded state. The system analyzes low microliter amounts of material collected directly from a column purification without having to dilute or dialyze the sample. Functionality of the material can be easily tested and results generated in three minutes, removing the guesswork out of analyzing protein complexes.
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Most recent content
Validation of Tycho NT.6 precision and repeatability
Protein labeling – improved quantitation of biomolecular interactions by MST using the His-Tag labeling kit RED-tris-NTA 2nd generation
Monitoring the impact of storage-dependent denaturation on protein quality using Tycho NT.6
Repeatability assessment of Tycho NT.6 for better protein quality checks
Quick protein binding analysis by label-free thermal shift analysis on the Tycho NT.6
Better optimization of biosensor assay development with Tycho NT.6
Evaluation of slow equilibration kinetics in antibody chemical denaturation experiments
Evaluating unfolding reversibility using temperature cycle measurements
Precision of measurements with the Prometheus NT.48