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Lunch and Learn with Nanotemper

August 28 @ 11:30 AM - 12:30 PM

Join ICBR Monoclonal Antibody and NanoTemper for a lunch and learn in CGRC 133. There will be a demo of the instrument in our Monoclonal Antibody lab after the seminar.

NanoDSF is a fast (3-60 min), label free technique that readily determines protein conformational and colloidal stability (aggregation) with high precision and resolution without limitations by protein size, concentration or buffer/detergent composition.The folded nature and conformational stability of your protein determines functionality, indicates proper storage conditions, helps select formulations for therapies or crystallography and select the best mutant or active molecules to work with. Case studies for these and other applications will be presented for the Tycho NT.6 and the Prometheus NT.48.

There will be a demonstration in the Monoclonal Antibody lab after the seminar from 1-4.  People can sign up ahead of time. If there are time slots open the day of the seminar, you can let us know your interest that day.  

For a successful demo there are several types of samples/experiments we recommend and some basic parameters:

  • A good fresh protein sample as a positive control that you know is active and you know what buffer it is in.
  • Concentration can be 10ug/ml -250mg/ml (yes,milligrams) but over 100ug/ml is best when things are unknown and if you can spare it.
  • 10ul + a couple extra for vile absorption is the minimum sample used per test/capillary.
  • Replicates are helpful to determine statistical significance when comparing samples with <1C  differences in melt temp. Due to this unknown, 40-50ul per sample is best if it can be spared.
  • Any buffer or additive can be used if it does not fluoresce in the 330-350nm region.
  • 2-3 proteins in the sample may be tolerated but it makes interpretation complex and sometimes impossible.  Purified samples of each component as controls should be tested to make this interpretation possible if at all.
  • When comparing samples they should be in the same buffer.  If this is an uncertainty, they should be buffer exchanged or highly diluted (1:100 or more) into the same buffer, so that Ti changes are not a result of varying buffers/pH. This applies to all of the experiments below.   
  • Comparative samples do not need to be at the same concentration, but it helps, because higher concentrations can cause oligimerization or aggregation which can change Ti. (eg BSA dimerizes).  Concentration dependency of stability is one application that you also can test.

You might perform the following applications:

    • Compare an older lot that has been freeze thawed multiple times, kept for a very long time, or mistreated (heat, acid, RT for a long period).
    • A Yes/No binding activity check of a Positive and negative control protein with and without known ligands (add ligand at or above affinity concentration).  The ligand should not fluoresce at 350-330 nm so typically protein-protein interactions are not possible unless one of the interactants lack Tryptophan and Tyrosine.
    • Stability of a mutant/variant compared to the control protein/wild type.
    • Fresh positive control protein in varying buffers and pH, especially conditions known to stabilize or destabilize, including highly basic or acidic.
    • Stability/melt temp dependency on concentration (due to oligomerization and Agg.)
    • Control protein vs heated/denatured sample.
    • If working with complexes, nanoparticles, liposomes, VLP, AAVs- choose samples that vary in one or more components to compare impact on thermal profile and conformational stability.


To sign up for the seminar, complete the form below.  To sign up for the demo: Click here


ICBR Seminars

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August 28
11:30 AM - 12:30 PM


(352) 273-8030


CGRC Room 133
2033 Mowry Road
Gainesville, FL 32610 United States
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