This webcast features: Gerald Platteau, Application Development Engineer, JSR Life sciences
Purification of full-length antibodies containing an Fc region relies on Protein A affinity chromatography as the golden standard capture step. The well-known robustness, high selectivity and scalability make it an ideal platform technique, minimizing downstream processing development time to bring new antibodies to market. After monoclonal antibodies (mAbs), various forms of antibody fragments are now becoming the next most important class of protein based therapeutics. These antibody fragments offer new biopharmaceutical opportunities, due to their structural, physiological, and pharmacological properties. Due to the lack of an Fc region, antibody fragments cannot be captured with most engineered Protein A domains. The Amsphere™ A3 Protein A ligand however exhibits high affinity to both the Fc-region as the VH3-region of IgGs. Amsphere™ A3 thus offers a Protein A affinity capture step for different VH/VHH containing antibody formats. In this webinar, Gerald Platteau explains the binding mechanism on a molecular basis for the binding of VH(H) antibody formats to Amsphere™ A3. Binding sites in the Protein A ligand and the VHH and VH molecules are identified and discussed. Dynamic binding capacity data of Amsphere™ for VHH single domain antibodies are compared to other affinity ligand resins in terms of dynamic binding capacity.
What you will learn:
- Antibody fragment types that can be purified with protein A resin
- Amsphere A3 binding sites in VHH single domain antibodies and VH domains
- Dynamic binding capacity data of Amsphere A3 for different antibody (fragment) formats
- Advantages of a Protein A resin for antibody fragment capture, compared to other resin types