Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties Publisher Pubmed



Soleimanpour S¹ ; Hassannia T² ; Motiee M³ ; Amini AA⁴ ; Rezaee SAR³
Source: Critical Reviews in Biotechnology Published:2017

Abstract

Affinity tags are vital tools for the production of high-throughput recombinant proteins. Several affinity tags, such as the hexahistidine tag, maltose-binding protein, streptavidin-binding peptide tag, calmodulin-binding peptide, c-Myc tag, glutathione S-transferase and FLAG tag, have been introduced for recombinant protein production. The fragment crystallizable (Fc) domain of the IgG1 antibody is one of the useful affinity tags that can facilitate detection, purification and localization of proteins and can improve the immunogenicity, modulatory effects, physicochemical and pharmaceutical properties of proteins. Fcγ recombinant forms a group of recombinant proteins called Fc-fusion proteins (FFPs). FFPs are widely used in drug discovery, drug delivery, vaccine design and experimental research on receptor–ligand interactions. These fusion proteins have become successful alternatives to monoclonal antibodies for drug developments. In this review, the physicochemical, biochemical, immunological, pharmaceutical and therapeutic properties of recombinant FFPs were discussed as a new generation of bioengineering strategies. © 2016 Informa UK Limited, trading as Taylor & Francis Group.