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Cloning of the functional domains of TSP-1 for protein expression

<p>Thrombospondin-1 (TSP-1) is a multifunctional extracellular matrix glycoprotein that is released from platelets α-granule to regulate angiogenesis process. TSP-1 is well-known as an inhibitory factor of angiogenesis that binds to angiogenesis stimulating factors, for example fibroblast growth factor 2 (FGF-2), vascular endothelial growth factor (VEGF) and hepatocyte growth factor/scatter factor (HGF/SF), to inhibit angiogenesis. We have cloned TSP-1 domains separately to allow studying of their function and effect on proliferation of human umbilical vein endothelial cells (HUVECs). We used an <em>Escherichia coli</em> expressionsvektor including poly histidin-tags and lac-promoter for induction of the seven successfully cloned domains by IPTG and arabinose. Our result shows that we have very low expression and induction of our protein in the <em>E.coli</em> by IPTG and arabinose, which is most likely due to complications associated with expressing a human protein in a prokaryotic system.</p>

Identiferoai:union.ndltd.org:UPSALLA/oai:DiVA.org:uu-107207
Date January 2009
CreatorsZangi, Shadi
PublisherUppsala University, Department of Medical Biochemistry and Microbiology
Source SetsDiVA Archive at Upsalla University
LanguageEnglish
Detected LanguageEnglish
TypeStudent thesis, text

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