[Bacterial overexpression of the human interleukin-2 in insoluble form via the pET Trx fusion system]
IJB-Iranian Journal of Biotechnology. 2010; 8 (4): 270-274
in English
| IMEMR
| ID: emr-145279
ABSTRACT
Selection of a system for successful recombinant protein production is important. The aim of this study was to produce high levels of human interleukin-2 [hIL-2] in soluble form. To this end, the pET32a vector in Escherichia coli BL21 [DE3] was used as an expression system, since it was previously used for the production of mouse IL-2 in soluble form. The results indicated that contrary to expectations, the expressed protein was in the form of inclusion bodies and perhaps amino acid differences between human and mouse IL-2 should be determinant. The hIL-2 protein is a small peptide, therefore its recovery as a biologically functional protein by the process of refolding may be feasible and could lead to high yields at the industrial scale
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Index:
IMEMR (Eastern Mediterranean)
Main subject:
Recombinant Proteins
/
Inclusion Bodies
/
Escherichia coli
Limits:
Animals
/
Humans
Language:
English
Journal:
Iran. J. Biotechnol.
Year:
2010
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