Fc-Fusion Protein Development - Creative Biolabs

Because of FcRn-mediated recycling, IgG molecules belonging to the IgG1, IgG2, and IgG4 subclasses have remarkably extended half-lives. Therapeutic antibodies have been reported to have half-lives as long as four weeks. The CH2 and CH3 domains combine to produce the binding site for FcRn, which is located in the Fc region. Therefore, a therapeutic protein can acquire the immunoglobulin-like half-life extension capabilities through fusing to an Fcγ region. Most fusion proteins have been developed via Fc fusion, which is one of the most clinically successful half-life extension techniques to date. Many different kinds of molecules, ranging in size from tiny peptides to bigger proteins, can be fused to the Fc region. Examples of these molecules are blood proteins, growth factors, hormones, and protein or peptide mimics.