Open AccessExpression, purification, and characterization of a diabody against the most important angiogenesis cell receptor: Vascular endothelial growth factor receptor 2
Author(s) -
Mahdi Behdani,
Sirous Zeinali,
Morteza Karimipour,
Hossein Khanahmad,
Nader Asadzadeh,
Kayhan Azadmanesh,
Negar Seyed,
Seyed Farzad Baniahmad,
Mahdi HabibiAnbouhi
Publication year - 2012
Publication title -
advanced biomedical research
Language(s) - English
Resource type - Journals
ISSN - 2277-9175
DOI - 10.4103/2277-9175.100126
Subject(s) - antibody , angiogenesis , receptor , vascular endothelial growth factor , kinase insert domain receptor , cancer research , metastasis , neovascularization , blockade , microbiology and biotechnology , chemistry , vegf receptors , biology , medicine , vascular endothelial growth factor a , cancer , immunology , biochemistry
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