Monoclonal antibodies (mAbs) used as therapeutics often require formulation at high concentrations to minimize administration volume. High concentration poses an increased risk of instability, primarily via complicated aggregation pathways. Identification of consistently reliable tools to predict longer term stability based on initial data remains a challenge in the biotech industry, especially in the context of protein aggregation. Aggregation is influenced by both colloidal and conformational stability. In this work, we evaluate the ability of these methods to predict the long-term aggregation for a series of mAbs based on their intrinsic molecular properties.