Measure the thermal stability of proteins through differential static light scattering

Using the label-free DSLS method pioneered by our scientists and engineers, Stargazer-2 measures the aggregation of protein in a 384-well microplate under controlled thermal conditions. This thermal aggregation assay can be used for many applications:
  • Thermal stability analysis of proteins using temperature scanning & isothermal methods
  • Formulation development of therapeutic monoclonal antibodies
  • Characterization of membrane proteins
  • Comparison of ligand specificity, including substrates, co-factors, inhibitors, etc.
  • Validation of HTS hits
  • Quality control of protein biologics
  • Focused library screening for buffer optimization, protein crystallization, chemical biology
  • Comparison of stability of SNP proteins
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NUNC 242764 showing measurable Xylanase aggregation.

Label-free technology

Stargazer-2 measures protein aggregation through the scattering of visible light. No fluorescent probes are used, meaning samples which were previously difficult to screen using DSF are now readily available using Stargazer-2's label-free technology.

Temperature gauge showing Stargazer-2 limits.

10°C-95°C Operation

384-well microplates, heating rates up to 5°C/minute and short cool-off times translate into high throughput and fast results.

A 10μL pipette tip with 2.5μL purple liquid.

Samples as low as 2.5μL

Using a standard, low-volume 384 well optical bottom microplate, Stargazer-2 is capable of simultaneously collecting data from up to 383 samples per experiment. Stargazer-2 can detect aggregation in samples as low as 2.5 μL/well with typical concentrations from 0.05 mg/mL to 1 mg/mL.

Fluorescent proteins or compounds getting in the way of DSF? Try Stargazer.

Stargazer-2's non-specific, label-free technology is unaffected by fluorescent samples. Contact us and discover the benefits of adding Stargazer to your lab bench.

Stargazer-2 DSLS Instrument

Stargazer-2 in a laboratory setting.

Next-generation differential static light scattering

We took the original Stargazer-384 instrument and redesigned the hardware and software from scratch. The result is Stargazer-2 — faster, more accurate, and easier to use.

Advanced Software

Stargazer's Magellanic control software allows users to customize the operation of Stargazer-2 to their needs with method-based experiments.

Stargazer-AIR automatically processes experiment results and provides the user with an intuitive graphical interface to review their results.

A modular plugin architecture allows users to export results to Excel and BioActive. LIMS integration is possible with custom plugins.

Online software updates ensure the best user experience.

Stargazer-2 AIR Software showing aggregation


Scattering wavelength
620nm (other wavelengths, inquire)
Sample temperatures
10 - 95ºC, 0.1 - 5.0ºC/minute
Number of samples
1 - 383 samples (well A24 reserved)
Sample volume
2.5 - 50μL (average 0.1 mg/mL concentration)
Protein consumption
100μg / microplate (383 x 2.5μL @ 0.1 mg/mL)
Approved microplates
Corning 3540, Nunc 242764
Physical dimensions
40 x 43 x 75cm (W x D x H), 50kg
10A, 100-240VAC, 50-60Hz, 1 Φ
Included Software
Stargazer-Magellanic, Stargazer-AIR
Computer requirements
Two USB 2.0 ports available, 3 GB RAM minimum

Selected Publications

  1. Vedadi M, Niesen FH, Allali-Hassani A, Fedorov OY, Finerty PJ Jr, Wasney GA, Yeung R, Arrowsmith C, Ball LJ, Berglund H, et al.
    2006. Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc Natl Acad Sci U S A. 103(43):15835-40.
  2. Senisterra GA, Markin E, Yamazaki K, Hui R, Vedadi M, Awrey DE.
    2006. Screening for ligands using a generic and high-throughput light-scattering-based assay. J Biomol Screen. 11(8):940-8.
  3. Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, et al.
    2007. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol Biochem Parasitol. 151(1):100-10.
  4. Hong BS, Senisterra G, Rabeh WM, Vedadi M, Leonardi R, Zhang YM, Rock CO, Jackowski S, Park HW.
    2007. Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorder. J Biol Chem. 282(38):27984-93.
  5. Senisterra GA, Ghanei H, Khutoreskaya G, Dobrovetsky E, Edwards AM, Privé GG, Vedadi M.
    2010. Assessing the stability of membrane proteins to detect ligand binding using differential static light scattering. J Biomol Screen. 15(3):314-20.
  6. Abdelsattar M. Omar, Mahmoud A. Elfaky, Stefan T. Arold, Sameh H. Soror, Maan T. Khayat, Hani Z. Asfour, Faida H. Bamane and Moustafa E. El-Araby.
    2020. 1H-Imidazole-2,5-Dicarboxamides as NS4A Peptidomimetics: Identification of a New Approach to Inhibit HCV-NS3 Protease. Biomolecules 2020, 10(3), 479.
  7. Moustafa E. El-Araby, Abdelsattar M. Omar, Sameh H. Soror, Stefan T. Arold, Maan T. Khayat, Hani Z. Asfour, Faida Bamane, Mahmoud A. Elfaky.
    2020. Synthetic bulky NS4A peptide variants bind to and inhibit HCV NS3 protease. Journal of Advanced Research 24 251-259.