• HTS of focused compound libraries
• Validation of HTS hits
• Buffer optimization
• Identification of ligands for protein crystallization
• QC of protein biologics
• Characterization of membrane proteins
• Comparison of stability of different constructs of a given protein, including SNPs [3].

• The thermal-aggregation assay is non-specific - i.e. it is not necessary to develop a dedicated assay for every protein.
• Because the instrument employs the classical principle of light scattering to measure aggregated protein, it is not susceptible intrinsic fluorescence in proteins or compounds.
• While differential scanning calorimetry can only be used to study one protein at a time, StarGazer-384 is designed for 384 samples in parallel.
• StarGazer-384 has integrated software for image processing, graphical visualization and numerical analysis. The software automatically generates thermal-aggregation curves for all the samples and computes the T_agg representing each curve [1,2].

Contact us to find our more about our StarGazer-384 platereader.

1. Vedadi M et al. Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc Natl Acad Sci U S A. 2006 Oct 24;103(43):15835-40.
2. Senisterra GA et al. Screening for ligands using a generic and high-throughput light-scattering-based assay. J Biomol Screen. 2006 Dec;11(8):940-8.
3. Hong BS et al. Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorder. J Biol Chem. 2007 Sep 21;282(38):27984-93.