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Soluble expression and one-step purification of recombinant mouse interferon-λ3 in Escherichia coli.

Authors
  • Wang, Y Q
  • Zhou, M
  • Zeng, L M
  • Gao, Q Y
  • Yuan, X L
  • Li, Y
  • Li, M C
Type
Published Article
Journal
Biochemistry (Moscow)
Publisher
Pleiades Publishing
Publication Date
Feb 01, 2015
Volume
80
Issue
2
Pages
228–232
Identifiers
DOI: 10.1134/S0006297915020091
PMID: 25756537
Source
Medline
License
Unknown

Abstract

Interferon (IFN)-λ3, a member of the type III IFN family, is a pleiotropic cytokine that exhibits potent antiproliferative, antiviral, and immunoregulatory activities. For further functional study of IFN-λ3, we developed an efficient procedure that includes cloning, expression, and purification to obtain relatively large quantity of mouse IFN-λ3 fusion protein. The mature IFN-λ3 protein-coding region was cloned into the prokaryotic expression vector pET-44. IFN-λ3 contains a hexahistidine tag at its C-terminus. We used Ni(2+)-nitrilotriacetic acid agarose-affinity chromatography to purify the expressed soluble protein. The purified IFN-λ3 inhibited significantly IL-13 production in stimulated RAW264.7 macrophages. Our findings show that the production of soluble IFN-λ3 proteins by the pET-44 vector in Escherichia coli is a good alternative for the production of native IFN-λ3 and could be useful for the production of other IFN proteins.

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