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[Prokaryotic expression, purification, and identification of recombinant human IL-11 protein].

Zhejiang Provincial Key Lab for Model Organisms, Wenzhou Medical College, Wenzhou 325035, China.
Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi 06/2012; 29(3):530-3.
Source: PubMed

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.

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