| Literature DB >> 34199525 |
Takeru Ebihara1, Jian Xu2, Yoshino Tonooka1, Takumi Nagasato1, Kohei Kakino1, Akitsu Masuda1, Kosuke Minamihata3, Noriho Kamiya3,4, Hirokazu Nakatake5, Yuuka Chieda5, Hiroaki Mon1, Tsuguru Fujii6, Takahiro Kusakabe1, Jae Man Lee6.
Abstract
The tumor necrosis factor α (TNFα) has been employed as a promising reagent in treating autoimmunity and cancer diseases. To meet the substantial requirement of TNFα proteins, we report in this study that mature types of recombinant human and murine TNFα proteins are successfully expressed in the baculovirus expression system using silkworm larvae as hosts. The biological activities of purified products were verified in culture murine L929 cells, showing better performance over a commercial Escherichia coli-derived murine TNFα. By comparing the activity of purified TNFα with or without the tag removal, it is also concluded that the overall activity of purified TNFα cytokines could be further improved by the complete removal of C-terminal fusion tags. Collectively, our current attempt demonstrates an alternative platform for supplying high-quality TNFα products with excellent activities for further pharmaceutical and clinical trials.Entities:
Keywords: TNFα; baculovirus; protein purification; silkworm expression system
Year: 2021 PMID: 34199525 DOI: 10.3390/insects12060517
Source DB: PubMed Journal: Insects ISSN: 2075-4450 Impact factor: 2.769