The mutant was overexpressed in Escherichia coli BL21(DE3) by IPTG induction.
IPTG诱导突变体在大肠杆菌BL21（DE3）中高效表达。
The modified gene was expressed by IPTG induction and purified by affinity chromatography and cleavage in place.
IPTG诱导该基因的表达，亲和层析和原位裂解法纯化表达产物。
After optimizing prokaryotic expression conditions, we determined the optimum inducement time and concentration of IPTG.
通过优化原核表达条件，确定了原核表达的最佳诱导时间和诱导剂浓度。
The different conditions, such as culture media, induced time and dosage of IPTG, were used to improve the target protein expression level.
为了提高目标蛋白的表达水平，进行了条件优化，诸如培养基、诱导时间和诱导剂量。
The ABP1 and TIR1 prokaryotic expression vectors were transformed into expression host strain BL21 (DE3), then after, IPTG was added to induce expression.
将构建好的ABP1及TIR1原核表达载体，转化表达宿主菌bl21 (DE3)，加入诱导物iptg进行诱导表达。
Fusion protein expression was induced by IPTG. After renaturation, the protein was purified by affinity chromatography and the bioactivity was examined by ELISA.
IPTG诱导表达融合蛋白，包涵体蛋白经复性后亲和层析法纯化，ELISA方法测定蛋白活性。
The recombinant plasmids containing mutant genes were transformed into the Escherichia coli strain BL21 (DE3), and the expressed proteins were found to be water soluble after the induction of IPTG.
将含突变基因的重组质粒转化大肠杆菌菌株bl2 1 (DE3)，经IPTG诱导表达获得的目的蛋白质均以可溶形式存在。
The recombinant plasmids containing mutant genes were transformed into the Escherichia coli strain BL21 (DE3), and the expressed proteins were found to be water soluble after the induction of IPTG.
将含突变基因的重组质粒转化大肠杆菌菌株bl2 1 (DE3)，经IPTG诱导表达获得的目的蛋白质均以可溶形式存在。
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