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ORIGINAL ARTICLE
Year : 2012  |  Volume : 1  |  Issue : 1  |  Page : 34

Expression, purification, and characterization of a diabody against the most important angiogenesis cell receptor: Vascular endothelial growth factor receptor 2


1 Department of Molecular Medicine, Pasteur Institute of Iran, Tehran, Iran
2 Department of Molecular Medicine, Pasteur Institute of Iran; Department of Anatomical Sciences, Division of Genetics and Molecular Biology, Faculty of Medicine, Isfahan University of Medical Sciences, Iran
3 Department of Animal Breeding and Genetics, Animal Science Research Institute of Iran, Tehran, Iran
4 Department of Virology, Pasteur Institute of Iran, Tehran, Iran

Correspondence Address:
Hossein Khanahmad
Department of Anatomical Sciences, Division of Genetics and Molecular Biology, Faculty of Medicine, Isfahan University of Medical Sciences, Isfahan
Iran
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/2277-9175.100126

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Antibodies and their derivative fragments have long been used as tools in a variety of applications, in fundamental research work, biotechnology, diagnosis, and therapy. Camels produce single heavy-chain antibodies (VHH) in addition to usual antibodies. These minimal-sized binders are very robust and bind the antigen with high affinity in a monomeric state. Vascular endothelial growth factor recepror-2 (VEGFR2) is an important tumor-associated receptor that blockade of its signaling can lead to the inhibition of neovascularization and tumor metastasis. Here, we describe the construction, expression, and purification VEGFR2-specific Diabody. Two variable fragments of a same camel anti-VEGFR2 antibody were linked together by the upper hinge segment of antibody to make a diabody. We showed the ability of diabody to recognition of VEGFR2 on the cell surface by FACS. Diabodies can be produced in the low-cost prokaryotic expression system, so they are suitable molecules for diagnostic and therapeutic issues.


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