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- W2019664555 abstract "A mature form of porcine interleukin-2 (IL-2) protein without signal peptides was expressed as glutathione S-transferase (GST) fusion proteins in Escherichia coli using pGEX vector. Since most of GST-IL-2 fusion protein was detected in an insoluble fraction on SDS-PAGE analysis, the insoluble fusion protein was solubilized by refolding procedure using urea. The recombinant IL-2 (rIL-2) was purified by a batch method using Glutathione Sepharose 4B and factor Xa digestion and used for preparation of antisera in mice. The antisera reacted with rIL-2 expressed in baculovirus system on immunoblot analysis. In addition, the purified rIL-2 showed a high biological activity on CTLL-2 proliferative response." @default.
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- W2019664555 date "2000-01-01" @default.
- W2019664555 modified "2023-09-25" @default.
- W2019664555 title "Expression of Porcine Interleukin-2 in Escherichia coli." @default.
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- W2019664555 doi "https://doi.org/10.1292/jvms.62.1101" @default.
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