Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli

We report a method for production of soluble heparin binding domain (HBD) of human vascular endothelial growth factor VEGF-A(165). Recombinant VEGF-A(165)-HBD that contains four disulphide bridges was expressed in specialised E. coli SHuffle cells and its activity has been confirmed through interact...

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Detalles Bibliográficos
Autores principales: Seyedarabi, Arefeh, Cheng, Lili, Zachary, Ian, Djordjevic, Snezana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3568127/
https://www.ncbi.nlm.nih.gov/pubmed/23409021
http://dx.doi.org/10.1371/journal.pone.0055690
Descripción
Sumario:We report a method for production of soluble heparin binding domain (HBD) of human vascular endothelial growth factor VEGF-A(165). Recombinant VEGF-A(165)-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.

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