Fc-Fusion proteins (also known as Fc chimeric fusion protein, Fc-Ig, Ig-based Chimeric Fusion protein and Fc-tag protein) are composed of the Fc domain of IgG genetically linked to a peptide or protein of interest. Fc-Fusion proteins have become valuable reagents for in vivo and in vitro research.
The Fc-fused binding partner can range from a single peptide, a ligand that activates upon binding with a cell surface receptor, signalling molecules, the extracellular domain of a receptor that is activated upon dimerization or as a bait protein that is used to identify binding partners in a protein microarray.
One of the most valuable features of the Fc domain in vivo, is it can dramatically prolong the plasma half-life (t1/2) of the protein of interest, which for bio-therapeutic drugs, results in an improved therapeutic efficacy; an attribute that has made Fc-Fusion proteins attractive bio-therapeutic agents.
In vitro applications of Fc-Fusion proteins include: immunohistochemistry, flow cytometry, binding assays and as Fc-Fusion baits in microarray technologies. In these applications, the Fc behaves like a supporting module where proteins can be attached whilst retaining their native biological activity. The Fc domain can also improve the in vivo and in vitro solubility and stability of some binding partners.
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