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Fcγ1 fragment of IgG1 as a powerful affinity tag in recombinant Fc-fusion proteins: immunological, biochemical and therapeutic properties.

Authors
  • Soleimanpour, Saman1
  • Hassannia, Tahereh2
  • Motiee, Mahdieh3
  • Amini, Abbas Ali4
  • Rezaee, S A R3
  • 1 a Microbiology & Virology Research Center, Bu-Ali Research Institute, Mashhad University of Medical Sciences , Mashhad, Iran. , (Iran)
  • 2 b Internal medicine Department, Arash Hospital, the College of Medicine, Tehran University of Medical Sciences , Tehran, Iran. , (Iran)
  • 3 c Inflammation and Inflammatory Diseases Research Center, Medical School, Mashhad University of Medical Sciences , Mashhad, Iran. , (Iran)
  • 4 d Department of Immunology, faculty of medicine, Kurdistan University of Medical Sciences , Sanandaj, Iran. , (Iran)
Type
Published Article
Journal
Critical reviews in biotechnology
Publication Date
May 01, 2017
Volume
37
Issue
3
Pages
371–392
Identifiers
DOI: 10.3109/07388551.2016.1163323
PMID: 27049690
Source
Medline
Keywords
License
Unknown

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.

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