表达产物用亲和层析一步法进行纯化，然后用凝胶阻滞试验观察重组蛋白结合质粒的能力。
The expressed protein was purified by one-step affinity chromatography, and its ability of binding plasmid was investigated via gel retardation experiments.
介绍了近年来重组蛋白质的常用表达系统以及各种分离纯化技术等研究和应用的进展情况。
The study and application were introduced on the expression system in common use and separation and purification technique of recombinant proteins in recent years.
以纯化的重组蛋白建立了初步的间接ELISA方法。
An indirected ELISA was established with the purified recombinant protein.
纯化的重组蛋白纯度约为93%。
The purified recombinant protein reached a purity of about 93%.
采用蛋白质分子量标准物和纯化的重组蛋白质进行半干式蛋白质印迹，探讨半干式电泳印迹的多种因素对印迹效果的影响。
To elucidate the effect of the semi-dry electrophoretic transfer and its influencing factors in Western blot, the protein marker and purified recombination protein were used to analyzed.
SDS电泳分析结果表明EPSPS重组蛋白的表达量在55%以上，纯化的EPSPS重组蛋白纯度可以达到90%。
The SDS gel electrophoresis analysis shows that the expression of EPSPS recombined protein is over 55% and the purified EPSPS recombined protein reached as 90%.
目的在大肠埃希菌中表达人神经元正五聚蛋白2 (NPTX2)，并对该重组蛋白进行纯化、鉴定。
Objective to construct the prokaryotic expression vector of human neuronal pentraxin 2 (NPTX2) gene, induce the expression of the recombinant fusion protein in e.
目的构建人高迁移率族蛋白1（HMGB1）编码基因的表达载体，获得纯化的重组蛋白，研究其生物学功能。
Objective To construct the recombinant vector, the expression of human HMGB1 code gene and to study its function.
利用镍柱亲和层析对表达的重组蛋白进行纯化，经SDS-PAGE及薄层扫描分析表明，重组蛋白的纯度在90%以上；
The recombinant protein was purified through Ni-chelating affinity chromatography, and the purity was above 90% explained by SDS-PAGE gel scan analysis.
通过裂解、洗涤、变性、复性等方法对包涵体蛋白进行处理，以电泳切胶回收所获得的纯化产物作为抗原，免疫小鼠制备抗重组蛋白血清。
The recombination fusion protein was purified by lysis, washing, denaturation and renaturation. The specific band of expression was excised from the gel and used to immunize mice .
结论：原核表达载体的构建、重组蛋白的表达、纯化及多克隆抗体的制备为今后研究该蛋白的功能提供了良好的基础。
CONCLUSION: Recombined prokaryotic expression vector, the purified protein and prepared polyclonal antibody were the necessary materials for further study of this protein.
目的克隆人促甲状腺激素受体胞外段基因，构建重组真核表达质粒，获得具有免疫学活性的纯化重组蛋白。
Objective to clone and construct the plasmid containing human thyroid stimulating hormone receptor (TSHR) gene ectodomain, and then identify the immunoreactivity of the purified recombinant protein.
HEV结构区ORF2蛋白在甲醇营养型酵母中的成功表达，以及初步纯化得到的具有强免疫学活性的重组蛋白，为研制新型戊型肝炎基因工程疫苗奠定了基础。
The successful expression of HEV ORF2 protein in p. Pastoris and the production of recombinant protein provides basis for genetically engineered vaccine development of hepatitis E.
HEV结构区ORF2蛋白在甲醇营养型酵母中的成功表达，以及初步纯化得到的具有强免疫学活性的重组蛋白，为研制新型戊型肝炎基因工程疫苗奠定了基础。
The successful expression of HEV ORF2 protein in p. Pastoris and the production of recombinant protein provides basis for genetically engineered vaccine development of hepatitis E.
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