IPTG

Firstly , it could use other inducers instead of IPTG .

其一，选用其他诱导剂替代IPTG。

Coli cells and the fusion protein was expressed after IPTG induction .

酶切分析和测序鉴定后，将阳性重组子质粒转入不同的大肠杆菌宿主细胞中进行融合表达。

The soluble expression was obtained when induced by IPTG at 30 ℃ .

重组蛋白在30℃诱导获得可溶表达。

IPTG was used to induce the expression .

用IPTG诱导表达。

Induced by IPTG , was inclusion body protein .

通过IPTG诱导，获得包涵体表达蛋白。

The recombinant protein was expressed by the inducing of IPTG .

通过IPTG诱导，在大肠杆菌中表达了重组番鸭IL-2蛋白。

Inclusion bodies were formed after recombinant induction by IPTG .

重组大肠杆菌经IPTG诱导形成了包涵体。

Induced by IPTG , the vector could express cyclin D1 protein in vitro .

经IPTG诱导，可正确表达蛋白。

Protein was induced by IPTG to express .

蛋白经IPTG诱导表达。

The protein expression of recombinant was little after induction with IPTG identified by SDS-PAGE .

对该重组菌株进行诱导表达，通过SDS-PAGE分析发现，目标酶蛋白表达量不多。

It indicated that optimal induced temperature was 30 C , whereas the change of IPTG concentration had little effect .

结果表明：最佳诱导温度为30℃，而IPTG的浓度变化对重组蛋白的表达量影响不大。

Finally , the optimization of expression conditions , such as temperature , concentration of IPTG and media , were studied .

优化诱导表达的条件，如温度、IPTG浓度、适用的培养基，探讨不同温度下蛋白的表达形式；

The culture conditions including IPTG concentration and expression time were optimized . The expression products were in forms of inclusion .

对表达中所需的IPTG浓度和时间进行优化，表达产物为包涵体形式。

Soluble expression product was in its highest content when IPTG was 0.1 mM and temperature was 15 ℃ .

在IPTG为0.1mM，培养温度为15℃时可溶性表达产物含量最高。

Coli strain and induced by IPTG .

coli菌株，IPTG诱导表达。

IPTG concentration and induction time have little effect on protein expression , but induction temperature can greatly affect the target protein expression level .

IPTG浓度和诱导时间对BmDichaete蛋白的表达影响不大，但诱导温度会显著影响目的蛋白的表达量。

The expression of recombinant protein was induced in the prokaryotic expressing system with high effectiveness by the addition of IPTG .

经IPTG诱导，RGD-蛛丝蛋白多聚物在原核系统高效表达。

Expression of fusion protein in Escherichia coli Rosetta was detected after induction by IPTG .

在IPTG诱导下，观察融合蛋白在大肠杆菌Rosetta中的表达情况；

The Escherichia coli containing recombinant vector expressed fusion protein of 36 KD after induction by IPTG .

含重组质粒的大肠杆菌在IPTG诱导下表达了特异性的融合蛋白，其分子量为36kD；

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。

SDS-PAGE analyzed the purity of protein through the purification of Ni-NTA resin after IPTG induction .

用Ni-NTA树脂纯化出目的蛋白，SDS-PAGE电泳分析其纯度，并初步分析目的蛋白活性。

After induced by IPTG , a 145 kDa protein in size was detected on SDS-PAGE gel .

经IPTG诱导后，经SDS-PAGE检测发现，产生145kDa的目的蛋白质。

After optimizing of induction time , IPTG concentration and induction length , the enzyme activity increased to 90 times of original strain .

通过对IPTG诱导时机、诱导浓度和诱导时间的优化研究，重组菌产生的比酶活进一步提高至酶源菌的90倍。

Effect of induce concentration , time and temperature of IPTG on the expression of the GST-GnRH / TRS gene

IPTG诱导浓度、时间及温度对重组促性腺激素释放激素基因表达的影响

Clones of higher expression level were selected , and grown in the presence of IPTG at 37 C to induce expression .

挑选出表达量最高的克隆子，然后于37℃经IPTG诱导表达。

Coli and was induced by IPTG .

coli并用IPTG进行诱导表达。

Expression of E protein by the transformants was induced by IPTG and analyzed by SDS-PAGE and Western blot .

经异丙基巯基半乳糖（IPTG）诱导表达后，十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDSpage）和蛋白免疫印迹分析表达产物。

Coli BL 21 ( DE3 ), and expressed by IPTG induction .

构建的重组表达质粒转化至大肠杆菌BL21（DE3），用IPTG诱导表达；

Coli BL21 ( DE3 ) for expression under the induction of IPTG .

将其转化表达菌BL21（DE3）并用IPTG进行诱导表达。

The expression level reached 6.66U/mg protein after IPTG inducing , which is 50 times higher than that of original strain .

重组菌在IPTG诱导下，表达出的重组蛋白比酶活量为666U/mg，比出发菌株高50倍。