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• W2072474557 abstract "Interleukin (IL)-25 (also known as IL-17E) is a distinct member of the IL-17 cytokine family which induces IL-4, IL-5, and IL-13 expression and promotes pathogenic T helper (Th)-2 cell responses in various organs. IL-25 has been shown to have crucial role between innate and adaptive immunity and also a key component of the protection of gastrointestinal helminthes. In this study, to produce bioactive recombinant human IL-25 (rhIL-25), the cDNA of mature IL-25 was performed codon optimization based on methylotropic yeast Pichia pastoris codon bias and cloned into the expression vector pPICZαA. The recombinant vector was transformed into P. pichia strain X-33 and selected by zeocin resistance. Benchtop fermentation and simple purification strategy were established to purify the rhIL-25 with about 17 kDa molecular mass. Functional analysis showed that purified rhIL-25 specifically bond to receptor IL-17BR and induce G-CSF production in vitro. Further annexin V-FITC/PI staining assay indicated that rhIL-25 induced apoptosis in two breast cancer cells, MDA-MB-231 and HBL-100. This study provides a new strategy for the large-scale production of bioactive IL-25 for biological and therapeutic applications." @default.
• W2072474557 created "2016-06-24" @default.
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• W2072474557 date "2013-10-08" @default.
• W2072474557 modified "2023-10-06" @default.
• W2072474557 title "Codon optimization, expression, purification, and functional characterization of recombinant human IL-25 in Pichia pastoris" @default.
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• W2072474557 doi "https://doi.org/10.1007/s00253-013-5264-4" @default.
• W2072474557 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3838785" @default.
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