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

摘要

We have constructed and expressed recombinant chimeric soluble TGF-beta type II receptor fused with the Fc portion of human IgG1 (sT beta R11-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 cytornegalovirus 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 sT beta R11-Fc binds native TGF-beta 1 and TGF-beta 3 isoforms and neutralizes their activity in vitro.