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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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
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author Seyedarabi, Arefeh
Cheng, Lili
Zachary, Ian
Djordjevic, Snezana
author_facet Seyedarabi, Arefeh
Cheng, Lili
Zachary, Ian
Djordjevic, Snezana
author_sort Seyedarabi, Arefeh
collection PubMed
description 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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spelling pubmed-35681272013-02-13 Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli Seyedarabi, Arefeh Cheng, Lili Zachary, Ian Djordjevic, Snezana PLoS One Research Article 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. Public Library of Science 2013-02-08 /pmc/articles/PMC3568127/ /pubmed/23409021 http://dx.doi.org/10.1371/journal.pone.0055690 Text en © 2013 Seyedarabi et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Seyedarabi, Arefeh
Cheng, Lili
Zachary, Ian
Djordjevic, Snezana
Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli
title Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli
title_full Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli
title_fullStr Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli
title_full_unstemmed Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli
title_short Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A(165)-Heparin Binding Domain in Escherichia coli
title_sort production of soluble human vascular endothelial growth factor vegf-a(165)-heparin binding domain in escherichia coli
topic Research Article
url 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
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