Production of soluble human vascular endothelial growth factor VEGF-A165-heparin binding domain in Escherichia coli

PLoS One. 2013;8(2):e55690. doi: 10.1371/journal.pone.0055690. Epub 2013 Feb 8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Binding Sites
  • Chromatography, Gel
  • DNA Primers
  • Escherichia coli / genetics*
  • Heparin / metabolism*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Vascular Endothelial Growth Factor A / biosynthesis
  • Vascular Endothelial Growth Factor A / genetics*
  • Vascular Endothelial Growth Factor A / metabolism

Substances

  • DNA Primers
  • Recombinant Proteins
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • Heparin