Related Experiment Video
Updated: Nov 22, 2025
A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
Improved secretion of recombinant human IL-25 in HEK293 cells using a signal peptide-pro-peptide domain derived from
Michael J Mullin1,2, Claire Wilkinson3,4, Ian Hiles5,4
1Protein Technologies Group, GlaxoSmithKline Research & Development, Gunnels Wood Road, Stevenage, SG1 2NY, Hertfordshire, UK. Michael.J.Mullin@gsk.com.
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.
Conclusion:
The Trypsin-1 signal peptide-pro-peptide sequence increased human IL-25 expression and secretion in mammalian cells by fivefold.
