Fc-Fusion Protein Development

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, fusing to an Fcγ region confers on a therapeutic protein the immunoglobulin half-life extension features (larger size, FcRn recycling). Most fusion proteins have been developed via Fc fusion, which is one of the most clinically successful half-life extension techniques to date. Hormones, growth factors, and blood proteins are just a few examples of the many molecules that can be fused to the Fc region, ranging in size from tiny peptides to bigger proteins.

It goes without saying that Fc-fusion extends the half-life of drugs. With years of experience under its belt, Creative Biolabs has built a robust technology platform that provides all-in-one Fc-fusion development services. Our offerings comprise, but are not restricted to:

creating the gene that codes for the Fc-fused protein

Increasing the expression of the Fc-fused protein gene

Fc-fusion protein construction

Fc-fusion protein expression

Acquiring pure Fc-fusion proteins