Protagen Protein Services is pleased to inform you about our latest publication: Analysis of kinetic stability of proteins by DSC - Thermal domain stability and prediction of molecule shelf-life -

Protagen Protein Services is pleased to inform you about our latest publication: Analysis of kinetic stability of proteins by DSC - Thermal domain stability and prediction of molecule shelf-life -

presented by Dr. Adrian Moise, Natalie Perraudeau, Dr. Burkhard Fleckenstein

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Temperature-induced unfolding of monoclonal antibodies and other therapeutic proteins, analyzed by differential scanning calorimetry (DSC) is an indispensable tool for the identification of the candidates with the lowest tendency to denature or of the formulations that increase stability. These decisions usually take into account the thermodynamic stability, represented by the melting temperature (Tm) of the protein and enthalpy of unfolding, derived from equilibrium thermodynamic analysis.
However, the temperature induced denaturation of proteins is rarely reversible and equilibrium thermodynamic analysis of kinetically controlled processes will lead to erroneous conclusions.