Induced by IPTG, was inclusion body protein.
通过IPTG诱导，获得包涵体表达蛋白。
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。
Induced under IPTG, the target band appeared as expectlly on SDS-PAGE profile.
IPTG诱导表达后，SDS-PAGE显示出现目的条带，与预期结果一致。
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 expression condition of plasmid pET-tmcC has been explored, but at all the testing temperature, IPTG concentration and different hosts protein expression was not found.
将重组质粒转化至大肠杆菌宿主中，对目的蛋白进行诱导表达，并对诱导表达条件如温度、IPTG浓度等进行了优化。
The induction temperature, induction time, and IPTG concentration were also optimized by a series of experiments. Further purification modes of this protein were also explored.
同时还进行梯度实验分别对诱导的温度、时间和IPTG诱导时菌体浓度进行优化，并对蛋白的纯化方案进行摸索。
Through induced expressing and analyzing on various kinds of SDS-PAGE parameter including time, temperature and IPTG density, the result showed that the best induced time was 3~4 hours;
通过对表达载体的SDS-PAGE各种参数包括时间、温度和IPTG 浓度诱导表达分析，结果显示最佳诱导时间为3～4 小时；
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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