Proteins like immunoglobulin (IgGs) are prone to degradation by a variety of pathways. In this study, a stabilizing formulation for long-term storage of a panel of seven monoclonal IgGs was found using differential scanning calorimetry (DSC). In the chosen formulations, the IgGs were subjected to stress, accelerated and real-time storage, and analyzed by size exclusion chromatography to determine fragment and aggregate content, and fluorescence-activated cell sorting to measure immunoreactivity. All IgGs showed the greatest conformational stability near their isoelectric point which was enhanced by adding sorbitol, sucrose, glycine, and sodium chloride. Optimized formulations, found by DSC, containing 20 % sorbitol and 1 M glycine prevented IgG aggregation and fragmentation and conserved immunoreactivity against shear stress, multiple freeze-thaw cycles, accelerated storage at 37 A degrees C, and 12 months storage at 4 and -20 A degrees C. Relatively poor thermal stability of the antigen-binding fragment domain was shown to limit storage stability of IgGs. This study confirms the predictive power of DSC to find storage formulations which protect IgGs during stress and long-term storage from aggregation and degradation. Liquid formulations found in this study may have a broad utility for other IgGs.