title: Production of soluble human vascular endothelial growth factor VEGF-A165-heparin binding domain in Escherichia coli.
abstract: We report a method for production of soluble heparin binding domain (HBD) of human vascular endothelial growth factor VEGF-A165. Recombinant VEGF-A165-HBD that contains four disulphide bridges was expressed in specialised E. coli SHuffle cells and its activity has been confirmed through interactions with neuropilin and heparin. The ability to produce significant quantities of a soluble active form of VEGF-A(165)-HBD will enable further studies addressing the role of VEGF-A in essential processes such as angiogenesis, vasculogenesis and vascular permeability.
authors: Institute of Structural and Molecular Biology, University College London, London, UK.
authors: Arefeh
authors: A
authors: Seyedarabi
authors: Lili
authors: L
authors: Cheng
authors: Ian
authors: I
authors: Zachary
authors: Snezana
authors: S
authors: Djordjevic
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D002850:Chromatography, Gel; D017931:DNA Primers; D004926:Escherichia coli / Q000235:genetics*; D006493:Heparin / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D042461:Vascular Endothelial Growth Factor A / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism
chemical_list: D017931:DNA Primers; D011994:Recombinant Proteins; C467484:VEGFA protein, human; D042461:Vascular Endothelial Growth Factor A; D006493:Heparin