Cloning, expression and bio-activity assay of chimeric fusion protein sTNFRII-IgG Fc
Xu, C.-X.; Yao, L.-H.; Zu, D.; Chen, A.-J.; Huang, G.-J.; Zhang, Z.-Q.
Sheng Wu Gong Cheng Xue Bao 18(2): 178-181
Tumor necrosis factor (TNF) is a key cytokine in immunology system and is related to many human diseases. In order to inhibit the activity of TNF, cDNA coding for soluble TNF receptor II (sTNFRII) and human IgG Fc were linked using a flexible hinge. This gene was expressed in E. coli as a chimeric protein and purified by metal chelate chromatography. The results show that the fusion protein exists in the physiological form as a dimer, has the ability to bind with TNF and inhibits the cytotoxicity of TNF on L929 cells. Contrasting to monomer sTNFRII, the chimeric protein has an improved bioactivity, and displays potential prospects for research and application.