Fc-Fusion proteins (also known as Fc chimeric fusion proteins, Fc-Ig’s, Ig-based Chimeric Fusion proteins and Fc-tag proteins) 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.
Examples of Fc-fused binding partners include, but are not limited to, single peptides, ligands activated upon cell-surface receptor binding, signaling molecules, extracellular domains of receptors activated upon dimerization and bait proteins used to identify binding partners in protein microarrays.
One of the most valuable characteristics conferred by the Fc domain in vivo is the dramatic prolonging of the plasma half-life (t1/2) of the protein of interest, which for biotherapeutic drugs can result in improved therapeutic efficacy; an attribute that has made Fc-Fusion proteins attractive biotherapeutic agents.
In vitro applications of Fc-Fusion proteins include, amongst others, immunohistochemistry (IHC), flow cytometry (FC), protein binding assays and use as microarray baits. In these applications, the Fc domain behaves as a supporting module to which 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.
We’re excited to offer a large selection of Fc-Fusion proteins from our sister company Absolute Antibody, which specializes in engineering unique recombinant antibodies and proteins.