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nanoDSF Technology

Our thermostability measurements use nanoDifferential Scanning Fluorimetry (nanoDSF), a label‑free method that tracks intrinsic fluorescence during thermal unfolding.
1

Sample Preparation

Purified proteins are prepared in standard buffer conditions or customer-specified formulations.
2

Temperature Ramping

Samples are subjected to controlled temperature increases while monitoring fluorescence changes.
3

Melting Point Determination

The midpoint of the unfolding transition (Tm) is determined from the fluorescence data.
Curious about the underlying technique? See the wiki: nanoDSF.

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What you get

  • Tm (melting temperature): Primary stability metric
  • Onset temperature and transition width: Context on unfolding behavior
  • Clear ranking: Compare variants for developability decisions

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When to use

  • Selecting robust variants for storage and handling
  • Comparing formulations or mutations for stability impact
  • Pairing with binding or activity to balance function vs stability

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FAQs

nanoDSF reads intrinsic fluorescence, which comes from aromatic residues (tryptophan and tyrosine) in the hydrophobic core. Proteins with those residues give a clear unfolding transition. Some de novo miniproteins do not carry enough aromatic content to produce a strong signal, and may show a weak or absent transition. See the nanoDSF wiki page.
Room temperature to 95 degrees Celsius.
Yes, and it is the cheaper way to do it. Adding thermostability to designs we have already expressed for a binding run is priced as an add-on, because it reuses the same material. Ask us to quote the combined scope.
Ready to set up a thermostability assay? Visit start.adaptyvbio.com/thermostability.