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Purification and characterization of recombinant human interleukin-29 expressed in Escherichia coli
- Source :
-
Journal of Biotechnology . Apr2006, Vol. 122 Issue 3, p334-340. 7p. - Publication Year :
- 2006
-
Abstract
- Abstract: Human interleukin (IL)-29 is the latest member of the class II cytokine family. However, as a result of lacking efficient method to generate relatively large quantity of IL-29, little is known of its functions in man. In the present study, an Escherichia coli expression system for the rapid expression of the human IL-29 gene was developed. It involved of cloning IL-29 gene into the pET-44 Ek/LIC vector, which allowed expression of IL-29 with a fusion tag consisting of the NusA protein, polyhistidine and S peptide (Nus-His-S-tag), and introducing a thrombin recognition site between the fusion tag and IL-29. The expressed fusion protein was purified by S-protein agarose affinity chromatography, and the fusion tag was removed from recombinant IL-29 by cleavage with thrombin. The purified IL-29 appeared a single band on SDS-PAGE, and the yield of IL-29 was 60mg from 1l of bacterial culture. N-terminal sequencing confirmed the identity of the purified protein. The recombinant IL-29 showed specific antiviral activity that was comparable to the commercially available IFN alfa-2b preparation. [Copyright &y& Elsevier]
- Subjects :
- *ESCHERICHIA coli
*HEMOSTATICS
*THROMBIN
*CELLULAR immunity
Subjects
Details
- Language :
- English
- ISSN :
- 01681656
- Volume :
- 122
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Journal of Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 20009836
- Full Text :
- https://doi.org/10.1016/j.jbiotec.2005.11.019