Transient expression of Fc-fused human glycoprotein 130 in Expi293F suspension cells.

Abstract

Human glycoprotein 130 (gp130) is a signal-transducing receptor for interleukin 6 (IL-6), whose signaling plays a critical role in chronic inflammation and cancer. The soluble form of gp130 specifically inhibits IL-6 trans-signaling. However, achieving high-level expression of a large glycoprotein such as gp130 is difficult. Here, we designed and constructed one Fc-gp130-pcDNA mammalian expression vector, with the mouse IgG2a Fc fragment added to the N-terminus of human gp130, which greatly increased the secretion of recombinant gp130 protein from Expi293F suspension cells. Recombinant fusion Fc-gp130 was easily and efficiently purified from the supernatant of transfected cells by one-step affinity chromatography. Moreover, Fc-gp130 could automatically form dimers by the disulfide bond. Fc-gp130 was confirmed as a more efficient IL-6 trans-signaling blocker by its higher biological activity against signal transducer and activator of transcription 3 (STAT3). This purified active Fc-gp130 could be used to develop valuable therapeutic agents against inflammatory diseases and cancers.

DOI: 10.1016/j.pep.2016.04.009

Cite this paper

@article{Zhao2016TransientEO, title={Transient expression of Fc-fused human glycoprotein 130 in Expi293F suspension cells.}, author={Xiaozhi Zhao and Wei Chen and Liyuan Ge and Wei Jiang and Bo Tang and Qing Zhang and Xiaoyu Xu and Chong Wang and Lin Cao and Hongqian Guo}, journal={Protein expression and purification}, year={2016}, volume={124}, pages={41-7} }