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• W2316059987 abstract "Abstract Interleukin 2 (IL-2) is a pharmacologically vital cytokine secreted mainly by activated CD4 + T lymphocyte. Recombinant human IL-2 (rhIL-2) protein has already been globally applied as an immune-therapeutic reagent for various diseases. Therefore, there is great interest in developing an active form of rhIL-2 in very large amounts and with excellent purity for clinical use. In this study, we successfully mass-expressed and purified N- or C-terminal tandem tag-fused rhIL-2 in a baculovirus expression vector system (BEVS) using silkworm larvae as factories. We confirmed that the intrinsic instability of hIL-2 causes the loss and low recovery of N-tagged rhIL-2 and that C-tagged rhIL-2 is more suitable for mass production. Furthermore, the activity of purified rhIL-2s was further validated by a cell proliferation assay of a human natural killer cell line, and both rhIL-2 proteins produced in the silkworm-BEVS exhibited comparable activity to that of the commercial E.coli -derived rhIL-2. Taken together, our results and strategies could contribute greatly to the mass production of active rhIL-2." @default.
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• W2316059987 date "2016-06-01" @default.
• W2316059987 modified "2023-09-29" @default.
• W2316059987 title "High-level expression and purification of biologically active human IL-2 using silkworm-baculovirus expression vector system" @default.
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• W2316059987 doi "https://doi.org/10.1016/j.aspen.2016.03.014" @default.
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