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Chemical and Thermal Stability Screening of an IgG1-Antibody

The main purpose in formulation development of biologicals, such as monoclonal antibodies, is to establish optimal conditions for long-term stability of the protein. 

Here we used the Prometheus NT.48 instrument by NanoTemper Technologies to perform a buffer screening for an IgG1-Antibody. This instrument uses nanoDSF technology to measure thermal and chemical stability as indicators to predict the best buffer conditions for the protein. 

The results show that thermal and chemical unfolding, together with short-term stability studies, provides a complementary screening tool for finding optimal buffer conditions.

Previous
nanoDSF: Label-free Thermal Unfolding Assay of G Protein-Coupled Receptors for Compound Screening and Buffer Composition Optimization
nanoDSF: Label-free Thermal Unfolding Assay of G Protein-Coupled Receptors for Compound Screening and Buffer Composition Optimization

Up next
nanoDSF Thermal Unfolding Analysis of Proteins Without Tryptophan Residues
nanoDSF Thermal Unfolding Analysis of Proteins Without Tryptophan Residues

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