Prokaryotic expression, purification, refolding and biological assays of recombinant human interleukin 4 inclusion body / 生物医学工程学杂志
Journal of Biomedical Engineering
;
(6): 866-869, 2007.
Article
in Chinese
| WPRIM
| ID: wpr-346053
ABSTRACT
A DNA fragment encoding human interleukin 4 was obtained by PCR from pORF-hIL4 plasmid. The amplified fragment was inserted into prokaryotic expression vector PQE60 and recombinant protein was expressed in E. Coli M15 by adding isopropyl-beta-D-thiogalactoside (IPTG). The hIL-4 protein was present as insoluble inclusion bodies in the bacterial extract. After denaturation of inclusion bodies with 5 mol/L guanidine hydrochloride, the supernate was diluted to get renaturized. Then dialysis and Ni chelating chromatography were used for purification. TF-1 proliferation assay of recombinant human interleukin 4 was performed, and then rhIL-4 was fit to be used for proliferation of human dendritic cells from monocyte in vitro.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Recombinant Proteins
/
Inclusion Bodies
/
Interleukin-4
/
Protein Folding
/
Escherichia coli
/
Genetic Vectors
/
Genetics
/
Metabolism
Limits:
Humans
Language:
Chinese
Journal:
Journal of Biomedical Engineering
Year:
2007
Type:
Article
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