<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>
Identifer | oai:union.ndltd.org:UPSALLA/oai:DiVA.org:uu-107207 |
Date | January 2009 |
Creators | Zangi, Shadi |
Publisher | Uppsala University, Department of Medical Biochemistry and Microbiology |
Source Sets | DiVA Archive at Upsalla University |
Language | English |
Detected Language | English |
Type | Student thesis, text |
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