The monoclonal antibodies and the recombinant antibody fragments are widely used in the biotechnology studies and in medicine as a powerful therapeutic and diagnostic tool. The most commonly used recombinant antibody fragments are single-chain fragment variable (scFv) because of their small size and minimal immunogenicity while still retaining high-affinity antigen binding. A wide range of expression systems such as bacterial and eukaryotic cell systems enable the sufficient production of scFv antibodies. However, their stable expression in soluble form and correct protein folding are often insufficient. In the present study, we present the autoinduction as a key element of the optimized scheme for heterologous expression of human monoclonal scFv antibodies (clones A1 and A12) in Escherichia coli HB2151, which resulted in two-fold increase of the total protein yield in 24 h.
Keywords: Autoinduction; Bacterial expression; Single-chain fragment variable (scFv).
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