Expression in yeasts and activity of recombinant GST-hunian soluble fibroblast growth factor receptor 1 fusion protein / 中国免疫学杂志

ABSTRACT

Objective: To express recombinant human soluble fibroblast growth factor receptor 1 ( sFGFR1) and study its antagonistic activity on FGF. Methods: Human sFGFR1 cDNA, isolated from human lung fibroblast cells with RT-PCR was confirmed by DNA sequencing and cloned into pYEX4T-1 yeast expression vector. The recombinant sFGFR1 was expressed in DY150 yeast cells and the product was identified by SDS-PAGE and Western blot. The activity of recombinant sFGFR1 was detected in N1H3T3 proliferation inhibition assay. Results: GSF-sFGFR1 fusion protein was expressed in yeast cells and was observed as a band of 60 Id) on a SDS- PAGE gel and by Western blot. The recombinant fusion protein was also found to be able to suppress FGF-induced proliferation of NIH3Th cells. Conclusion: Recombinant human GST-sFGFR1 fusion protein was expressed in yeast efficiently and showed natural biological activities.