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Related Experiment Video

Updated: Jul 15, 2026

High-throughput Quantitative Real-time RT-PCR Assay for Determining Expression Profiles of Types I and III Interferon Subtypes
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Published on: March 24, 2015

Purification and characterization of prokaryotically expressed human interferon-lambda2.

Mingcai Li1, Dongyang Huang

  • 1Allergy and Inflammation Research Institute, Shantou University Medical College, Shantou, Guangdong, PR China. mingcai_li@yahoo.com

Biotechnology Letters
|April 3, 2007
PubMed
Summary

Researchers developed a method to produce soluble interferon (IFN)-lambda2 using a fusion protein system in E. coli. The purified and biologically active IFN-lambda2 demonstrated antiviral properties comparable to commercial IFN-alpha2b.

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Development and Validation of an Ultrasensitive Single Molecule Array Digital Enzyme-linked Immunosorbent Assay for Human Interferon-α

Published on: June 14, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Interferon (IFN)-lambda2 is a cytokine with potential therapeutic applications.
  • Efficient production of soluble and active IFN-lambda2 is crucial for its clinical use.

Purpose of the Study:

  • To develop a system for the production and purification of soluble interferon (IFN)-lambda2.
  • To characterize the biological activity of the produced IFN-lambda2.

Main Methods:

  • A fusion protein strategy involving IFN-lambda2, NusA, polyhistidine, and S peptide was employed.
  • Expression in Escherichia coli followed by Ni-NTA affinity chromatography for purification.
  • Tag removal using enterokinase and N-terminal sequencing for protein identification.

Main Results:

  • A system for producing soluble Nus-His-S-tagged IFN-lambda2 was successfully established.
  • Purified recombinant IFN-lambda2 exhibited comparable antiviral activity to commercial IFN-alpha2b.
  • Protein identity was confirmed through N-terminal sequencing.

Conclusions:

  • The developed system enables the production of biologically active interferon (IFN)-lambda2.
  • This method facilitates the characterization of IFN-lambda2 for potential clinical applications.
  • Soluble IFN-lambda2 production is feasible and holds promise for therapeutic development.