Michael Williams

Webinar: The Benefits of Detecting Intrinsic Fluorescence

Differential Scanning Fluorimetry (DSF) is a valuable and widely-used technique that monitors protein unfolding with increasing temperature by detecting changes in fluorescence. However, the conventional workflow for DSF uses extrinsic dyes that may influence the protein's thermal stability under investigation. This can affect the quality of your data by generating false positives or negatives during screening. In this webinar, we’ll show you an alternative solution: SUPR-DSF. The SUPR-DSF avoids dyes by using the intrinsic fluorescence of a protein’s tryptophan or tyrosine residues to detect structural changes. This streamlines sample preparation and removes the risks associated with small-molecule dyes. It also maintains the high throughput possible with plate-based assays. This speeds protein and formulation screening and increases confidence in the results. We will discuss using Differential Scanning Fluorimetry (DSF) for assessing protein stability as part of candidate selection and formulation development. We’ll also consider the advantages of using intrinsic protein fluorescence as a detection method for DSF, with particular attention to the simplified workflow of the new SUPR-DSF system. Join us as we explain how SUPR-DSF could revolutionize your protein stability screening for drug discovery!

Who should attend? 

Scientists and researchers working on the discovery and development of biologics and small molecule drugs and interested in the following:

  • Construct Screening
  • Formulation Development 
  • Binding Affinities

What will you learn? 

  • Learn how to ensure data quality and increase your drug screening throughput  
  • Discover how to scan up to 384 samples in one single 90-minute experiment
  • Understand why DSF provides complementary data to other techniques