Various methods have been developed for their production. The fine-tuned design is suitable for the production of IgG-like BsAb with high symmetry between the two antigen-binding fragments that is advantageous for screening BsAbs.īispecific antibodies (BsAbs) are widely used as therapeutic agents and have been successful for example as T cell engagers 1, 2. Cleaved side product formation was inevitable, but it was minimized under the optimized conditions. A BsAb binding to both TNFR2 and CD30 was successfully produced. In this study, we designed a BsAb linked by IMPTS, without the extra Cys residue. An extra Cys residue is incorporated as a consensus sequence for IMPTS in successful examples, but this may lead to potential destabilization or disturbance of the assay system. One such method uses intein-mediated protein trans-splicing (IMPTS) to produce an IgG1-based structure. Because appropriate pairing of heavy and light chains is required, the design of BsAbs produced through recombination or reassembly of two separately-expressed antigen-binding fragments is advantageous. ![]() A major class of bispecific antibodies (BsAbs) utilizes heterodimeric Fc to produce the native immunoglobulin G (IgG) structure.
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