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Improved secretion of recombinant human IL-25 in HEK293 cells using a signal peptide-pro-peptide domain derived from Trypsin-1

Biotechnol Lett. 2021-01;

Michael J Mullin, Claire Wilkinson, Ian Hiles, Kathrine J Smith

Products/Services Used	Details	Operation
Gene Synthesis	… biology. Materials and methods. Vector constructs. hIL-25 (Uniprot Q9H293) expression constructs were made by a combination of in-house cloning using gBlocks? from IDT DNA and gene synthesis and sub-cloning at Genscript?…	Get A Quote

摘要

objective: To compare the effects of human Trypsin-1 signal peptide and pro-peptide on the expression and secretion efficiency of human Interleukin-25 from mammalian cells. results: The signal peptide and combined signal peptide-pro-peptide sequence of human Trypsin-1 improved the secretion of human IL-25 from 1.7 to 3.2?μg/ml and 1.7 to 8.2?μg/ml, respectively. Deletion analysis identified the minimal Trypsin-1 derived secretion domain that maintains improved human Interleukin-25 production and secretion. The presence of Trypsin-1 pro-peptide sequence does not affect the function of secreted human Interleukin-25. conclusions: The Trypsin-1 signal peptide-pro-peptide sequence increased human IL-25 expressio... More