Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A165-Heparin Binding Domain in Escherichia coli | Zendy

Arefeh Seyedarabi | Zendy; Lili Cheng | Zendy; Ian Zachary | Zendy; Snežana Djordjević | Zendy

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Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A165-Heparin Binding Domain in Escherichia coli

Author(s) -

Arefeh Seyedarabi,

Lili Cheng,

Ian Zachary,

Snežana Djordjević

Publication year - 2013

Publication title -

plos one

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.99

H-Index - 332

ISSN - 1932-6203

DOI - 10.1371/journal.pone.0055690

Subject(s) - vascular endothelial growth factor , angiogenesis , neuropilin 1 , vasculogenesis , heparin , vascular endothelial growth factor a , vegf receptors , chemistry , recombinant dna , microbiology and biotechnology , biochemistry , biology , cancer research , endothelial stem cell , in vitro , gene

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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