title: [Prokaryotic expression, purification, and identification of recombinant human IL-11 protein].
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.
authors: Zhejiang Provincial Key Lab for Model Organisms, Wenzhou Medical College, Wenzhou 325035, China.
authors: Jia
authors: J
authors: Tang
authors: Xiaoling
authors: X
authors: Xu
authors: Xiaoxia
authors: X
authors: Nie
authors: Qifeng
authors: Q
authors: Mao
authors: Jimin
authors: J
authors: Gao
mesh_terms: D004926:Escherichia coli / Q000378:metabolism; D005822:Genetic Vectors / Q000235:genetics; D006801:Humans; D017370:Interleukin-11 / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: C508611:IL11 protein, human; D017370:Interleukin-11; D011994:Recombinant Proteins