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[Production of recombinant hIL-4delta2-a native isoform of human interleukin-4 in Escherichia coli cells].

Ptitsyn Lr, Smirnov Sv, Al'tman Ib, Samsonova Nn, Khodiakova Av, Vasilenko Rn

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Abstract

Expression plasmids containing the synthetic gene hil-4 delta 2 was constructed to produce human interleukin-4 in Escherichia coli cells. Strains TG1 (pBTIL-4 delta 2) and BL21 (DE3) (pETIL-4 delta 2) produced the recombinant protein as inclusion bodies, and its production level was up to 30% of the total cell protein. The renatured hIL-4 delta 2 inhibited IL-4-stimulated T cell proliferation, and this effect was enhanced by cyclosporin A.

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What this paper is about

Expression plasmids containing the synthetic gene hil-4 delta 2 was constructed to produce human interleukin-4 in Escherichia coli cells. Strains TG1 (pBTIL-4 delta 2) and BL21 (DE3) (pETIL-4 delta 2) produced the recombinant protein as inclusion bodies, and its production level was up to 30% of the total cell protein. The renatured hIL-4 delta 2 inhibited IL-4-stimulated T cell proliferation, and this effect was enhanced by cyclosporin A.

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Available abstract

Expression plasmids containing the synthetic gene hil-4 delta 2 was constructed to produce human interleukin-4 in Escherichia coli cells. Strains TG1 (pBTIL-4 delta 2) and BL21 (DE3) (pETIL-4 delta 2) produced the recombinant protein as inclusion bodies, and its production level was up to 30% of the total cell protein. The renatured hIL-4 delta 2 inhibited IL-4-stimulated T cell proliferation, and this effect was enhanced by cyclosporin A.

Key concepts: Recombinant DNA, Escherichia coli, Plasmid, Inclusion bodies, Gene isoform, Chemistry, Molecular biology, Enterobacteriaceae

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[Production of recombinant hIL-4delta2-a native isoform of human interleukin-4 in Escherichia coli cells]. — Research Paper | ScholarLens