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Expression of soluble recombinant TGF-β type II receptor fused with the Fc portion of human IgG1 (sTβRII-Fc) in NS0 cells

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Kwiatkowska E. P., Kazimierczak U., Mackiewicz A., Kowalczyk D. W.
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2006
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vol. 53
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issue 2
361-369
EN
We have constructed and expressed recombinant chimeric soluble TGF-β type II receptor fused with the Fc portion of human IgG1 (sTβRII-Fc) in NS0 mouse myeloma cells and isolated cell lines constitutively secreting very high levels of biologically active protein. The GS-NS0 expression system takes advantage of the strong human cytomegalovirus immediate early promoter expression vector and glutamine synthetase as a selectable marker. The recombinant chimeric receptor could be produced in high amounts and efficiently purified by one step chromatography on a protein A column. Biochemical studies revealed that recombinant sTβRII-Fc binds native TGF-β1 and TGF-β3 isoforms and neutralizes their activity in vitro.
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