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

• Published in: Advanced biomedical research 2012, Vol.1 (1), p.34-34
• Main Authors: Behdani, Mahdi, Zeinali, Sirous, Karimipour, Morteza, Khanahmad, Hossein, Asadzadeh, Nader, Azadmanesh, Kayhan, Seyed, Negar, Baniahmad, Seyed Farzad, Anbouhi, Mahdi Habibi
• Format: Article
• Language: English
• Subjects: Antibodies; Cell receptors; Chemical properties; Diabody; Nanobody; Neovascularization; Original; Physiological aspects; Vascular endothelial growth factor; vascular endothelial growth factor recepror-2; Viral antibodies
• ISSN: 2277-9175; 2277-9175
• DOI: 10.4103/2277-9175.100126

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.