Prokaryotic expression, purification, and identification of recombinant human IL-11 protein / 生物医学工程学杂志
Journal of Biomedical Engineering
;
(6): 530-533, 2012.
Article
in Chinese
| WPRIM
| ID: wpr-271739
ABSTRACT
A DNA fragment encoding recombinant human interleukin 11 (hrIL-11) was obtained by PCR from previously constructed pET24a-hrIL-11 plasmid. Then pET21a-hrIL-11 expression vector was constructed routinely and transformed into BL-21(DE3). By the induction of Isopropyl-1-thio-beta-D-galactoside (IPTG), hrIL-11 protein was highly expressed at about 20% of the total bacterial proteins and was identified by Western blot. After purification with Ni-NTA affinity chromatography and refolding with renaturation buffer, the purity of the target hrIL-11 protein reached 95% and its biology activity was 1 x 10(6) IU/mg, determined by stimulating the proliferation of T1165, which facilitates further researches into effects of IL-11 on platelet proliferation and other function.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Recombinant Proteins
/
Interleukin-11
/
Escherichia coli
/
Genetic Vectors
/
Genetics
/
Metabolism
Type of study:
Prognostic study
Limits:
Humans
Language:
Chinese
Journal:
Journal of Biomedical Engineering
Year:
2012
Type:
Article
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