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Isolation of a Novel Anti-Kdr3 Single-Chain Variable Fragment Antibody From a Phage Display Library Publisher Pubmed



Kordi S1, 2 ; Rahmatiyamchi M2 ; Vostakolaei MA3 ; Etemadie A4 ; Barzegari A5 ; Abdolalizadeh J6, 7
Authors
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Authors Affiliations
  1. 1. Immunology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
  2. 2. Department of Medical Biotechnology, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran
  3. 3. Student Research Committee, Tabriz University of Medical Sciences, Tabriz, Iran
  4. 4. Department of Medical Biotechnology, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. Research Centre for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran
  6. 6. Faculty of Paramedicine, Tabriz University of Medical Sciences, Tabriz, Iran
  7. 7. Clinical Biochemistry, Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran

Source: Iranian Journal of Allergy# Asthma and Immunology Published:2019


Abstract

Vascular endothelial growth factor receptor 2 (VEGFR-2) is known as one of the important antigens playing a vital role in angiogenesis. In this study, phage display technology (PDT) was used to produce a single-chain variable fragment (scFv) antibody against a region of the domain 3 in VEGFR-2 called kinase insert domain receptor 3 (KDR3). After designing the KDR3 peptide and biopanning, a colony was chosen for scFv antibody expression. Following expression and purification; western blotting, dot blotting and immunofluorescence (IF) were used to evaluate the antibody function. Surface plasmon resonance (SPR) was also employed to measure affinity of produced antibody. Once a colony was selected and transferred to the expression host, the scFv antibody was expressed in the expected range of 28 kDa. Using a designed chromatography column, antibody purification was found to be about 95%. In this study, a novel scFv with the capability of binding to KDR3 was isolated and purified and its intracellular function was investigated and verified. Copyright © June 2019, Iran J Allergy Asthma Immunol. All rights reserved.
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