High Throughput Platforms to Characterize a Bispecific Antibody Subjected to Forced Degradation

The new bispecific antibody class (bsAbs) has emerged as one of the fastest-growing next-generation antibody therapies, due to its high specificity and low toxicity. bsAbs are designed to have two specific antigen-binding sites, unlike conventional antibody formats. Rapid and accurate functional evaluation methods and stability characterization are required to ensure product quality, safety, and efficacy.

In this study, we evaluated the stability of a bispecific mouse antibody targeting CD200 and CD47 in mouse, proteins over-expressed in many cancers, under heat stress conditions:

• High throughput HTRF^® with TR-FRET (Time-Resolved Fluorescence Resonance Energy Transfer) to evaluate the effect of heat stress on the binding activity of bsAbs.
• High throughput LabChip^® ProteinEXact^™ to evaluate the fragmentation of monoclonal antibodies after heat stress, and analyze different forms of bsAbs from cell culture supernatants.