Expression of soluble recombinant TGF-beta type II receptor fused with the Fc portion of human IgG1 (sTbetaRII-Fc) in NS0 cells.
Abstract
We have constructed and expressed recombinant chimeric soluble TGF-beta type II receptor fused with the Fc portion of human IgG1 (sTbetaRII-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 sTbetaRII-Fc binds native TGF-beta1 and TGF-beta3 isoforms and neutralizes their activity in vitro.Acta Biochimica Polonica is an OpenAccess quarterly and publishes four issues a year. All contents are distributed under the Creative Commons Attribution-ShareAlike 4.0 International (CC BY 4.0) license. Everybody may use the content following terms: Attribution — You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
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