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Related Experiment Videos

Expression of human interleukin-11 cDNA in E. coli

J Miao1, J Wang, S Peng

  • 1Institute of Basic Medical Sciences, Beijing, China.

Science in China. Series B, Chemistry, Life Sciences & Earth Sciences
|October 1, 1995
PubMed
Summary

Researchers successfully cloned and expressed human interleukin-11 (hIL-11) in E. coli. The resulting recombinant hIL-11 protein demonstrated significant biological activity, paving the way for potential therapeutic applications.

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Area of Science:

  • Molecular Biology
  • Biotechnology
  • Protein Expression

Background:

  • Human interleukin-11 (hIL-11) is a cytokine with significant biological functions.
  • Efficient and scalable production of recombinant hIL-11 is crucial for research and therapeutic development.

Purpose of the Study:

  • To clone and express a functional human interleukin-11 (hIL-11) gene fragment in Escherichia coli (E. coli).
  • To develop a method for purifying and renaturing the expressed recombinant hIL-11 protein.
  • To assess the biological activity of the purified recombinant hIL-11.

Main Methods:

  • Cloning of a 551-bp hIL-11 gene fragment into the pEx31B expression vector.
  • Transformation of E. coli strain HB101 and induction of protein expression using a temperature-regulated PL promoter system.

Related Experiment Videos

  • Purification of the expressed fusion protein (hIL-11 fused to MS2 polymerase) from inclusion bodies using urea extraction.
  • Bioassay using the IL-6-dependent cell line 7TD1 to determine specific activity.

    • Main Results:

    • A recombinant plasmid, pEx31-IL11, was successfully constructed and identified.
    • The expressed fusion protein constituted up to 50% of total bacterial proteins.
    • Recombinant hIL-11 was purified to approximately 80% purity.
    • The purified and renatured recombinant hIL-11 exhibited a specific activity of 10(5) U/mg, retaining activity in the presence of anti-IL-6 antibodies.

    Conclusions:

    • High-level expression of recombinant hIL-11 in E. coli is feasible.
    • The developed purification and renaturation protocol yields biologically active hIL-11.
    • This method provides a promising approach for producing recombinant hIL-11 for further studies and potential therapeutic use.