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

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

Show Affiliations

1. Microbiology & Virology Research Center, Bu-Ali Research Institute, Mashhad University of Medical Sciences, Mashhad, Iran
2. Internal medicine Department, Arash Hospital, College of Medicine, Tehran University of Medical Sciences, Tehran, Iran
3. Inflammation and Inflammatory Diseases Research Center, Medical School, Mashhad University of Medical Sciences, Mashhad, Iran
4. Department of Immunology, faculty of medicine, Kurdistan University of Medical Sciences, Sanandaj, Iran

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.

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Style	Citing Format
MLA	Soleimanpour S, et al.. "Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties." Critical Reviews in Biotechnology, vol. 37, no. 3, 2017, pp. 371-392.
APA	Soleimanpour S, Hassannia T, Motiee M, Amini AA, Rezaee SAR (2017). Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties. Critical Reviews in Biotechnology, 37(3), 371-392.
Chicago	Soleimanpour S, Hassannia T, Motiee M, Amini AA, Rezaee SAR. "Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties." Critical Reviews in Biotechnology 37, no. 3 (2017): 371-392.
Harvard	Soleimanpour S et al. (2017) 'Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties', Critical Reviews in Biotechnology, 37(3), pp. 371-392.
Vancouver	Soleimanpour S, Hassannia T, Motiee M, Amini AA, Rezaee SAR. Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties. Critical Reviews in Biotechnology. 2017;37(3):371-392.
BibTex	@article{ author = {Soleimanpour S and Hassannia T and Motiee M and Amini AA and Rezaee SAR}, title = {Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties}, journal = {Critical Reviews in Biotechnology}, volume = {37}, number = {3}, pages = {371-392}, year = {2017} }
RIS	TY - JOUR AU - Soleimanpour S AU - Hassannia T AU - Motiee M AU - Amini AA AU - Rezaee SAR TI - Fcγ1 Fragment of Igg1 As a Powerful Affinity Tag in Recombinant Fc-Fusion Proteins: Immunological, Biochemical and Therapeutic Properties JO - Critical Reviews in Biotechnology VL - 37 IS - 3 SP - 371 EP - 392 PY - 2017 ER -

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