Expression of a Recombinant Extracellular Fragment of Human Vascular Endothelial Growth Factor Receptor VEGFR1 in E. coli.

Bull Exp Biol Med. 2011 Jul; 151(3): 347-52
Leopold AV, Baklaushev VP, Pavlov KA, Chekhonin VP

Human vascular endothelium expansion cause receptor VEGFR1 is a type III fms-like tyrosine kinase with wrongly pronounced tyrosine kinase function. The second and third IgG-like domains of a extracellular part of VEGFR1 act as "traps" for VEGF and are prospective candidates for antiangiogenic therapy of VEGF-dependent tumors. cDNA encoding extracellular Ig-like domains 2, 3, 4 of VEGFR1 was cloned in expressing vectors pET28a, pET32a, and pQE60. The recombinant protein was expressed in E. coli cells and purified by metal affinity chromatography. An expressing construction and a superproducer strain were created, allowing a production of high amounts of recombinant VEGFR1 extracellular fragment, needed for initial in vivo antiangiogenic therapy.

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