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NanoTemper Technologies is deeply committed to the best customer experience. Central to this is a strong focus on enabling researchers to easily, efficiently, and accurately perform protein characterization.
With a broad offering of systems, software and consumables for evaluating binding affinities, protein stability, and protein quality, scientists in pharmaceutical, biotech or academic labs will find an optimized workflow, quality results, and responsive customer support.
Work with a deeply experienced and globally operating team, and realize the NanoTemper experience.
We have some great news! FOCUS and Statista have ranked the 500 fastest-growing companies in Germany and we made the list! They identified companies with exceptional growth rates between the years 2012 and 2015 as “Growth Champions 2017”. We’re proud to announce that NanoTemper Technologies ... > more
We have some great news! FOCUS and Statista have ranked the 500 fastest-growing companies in Germany and we made the list! They identified companies with exceptional growth rates between the years 2012 and 2015 as “Growth Champions 2017”. We’re proud to announce that NanoTemper Technologies ... more
A Revolution in Protein Stability Analysis
The assessment of thermal stability parameters of biologics is an integral part of biopharmaceutical research. The ever growing number of biologics in the development pipelines worldwide demands rapid and precise methods to quickly screen large sets of conditions in an easy and straightforw ... more
Assess Enzyme Stability without Buffer Limitations
Would you like to assess enzyme stability without any buffer restrictions? Read more about thermal unfolding analysis of an esterase in detergents more
nanoDSF Goes GPCR Characterization
Learn how nanoDSF evaluates compounds for lead discovery and improves receptor stability for biophysical assays by screening buffer conditions more
Predicting the Long-Term Stability of Biologics
Learn how to predict long-term mAb stability in a formulation screen by quantification of conformational and colloidal stability more
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