Overview of Antibody Purification
Since the discovery of antibodies, there have been various methods for the isolation and purification of antibodies. Scientists around the world have been exploring efficient methods for the isolation and purification of antibodies, as well as processes suitable for the large-scale production of antibody drugs. The preparation of highly specific and high-titer antibodies is the basis for immunological research and development of antibody drugs. Unpurified or poorly purified antibodies will directly affect the accuracy, stability and even the success or failure of experimental data.
Fig. 1 Structure of a typical immunoglobulin, IgG. (Arora, et al., 2017)
How to Purify Antibodies?
Polyclonal antibodies, monoclonal antibodies (mAbs) and antibody fragments are usually purified by affinity chromatography, that is, the antibodies and antibody fragments are captured on a carrier containing ligands (e.g., protein A, protein G). The binding of the ligand is reversible, and the target antibody is usually collected by elution by lowering the pH. This method is highly selective, with purity levels above 95%, and purification in one step.