原核融合

嗜肺军团菌flaA基因的克隆及原核融合表达

Cloning and Prokaryotic Expression of Flagellum Subunit Gene ( flaA ) of Legionella pneumophila

目的：从大鼠磨牙胚组织中克隆大鼠磨牙牙根发育相关基因mrp1，构建原核融合表达载体，利用大肠杆菌表达其C端肽。

AIM : To clone rat molar root patterning gene 1 ( mrp1 ) and construct prokaryotic expression vector . METHODS : The lower molar tissue of rat on the third postnatal day were removed and mRNA was obtained .

结论：原核融合表达的HAb18G胞外区片段可以替代天然的HAb18G蛋白，以用做抗原来筛选新型的基因工程抗体。

CONCLUSION : The extracellular domain of HAb18G expressed in prokaryotic expression system can substitute natural HAb18G protein as antigen to screen new type gene engineering antibody of HAb18G .

25min后，雌、雄性原核融合；

By the 25 min postinsemination , the male and female pronuclei are fused to form the nucleus of the zygote .

目的克隆家蝇幼虫Attacin抗菌肽基因，构建原核融合表达载体，建立Attacin体内抗菌活性检测系统，优化表达和纯化Attacin目的蛋白，并初步研究其抗菌生物学功能。

Objective To clone the cDNA sequence of Attacin gene from Musca domestica larvae , construct prokaryotic fusion expression vectors , express and purify the Attacin protein , and preliminarily study its antibiotic biological function .

重组人神经生长因子β亚基的原核融合表达及其活性研究

Fusion Expression of Recombinant Human Nerve Growth Factor β - Subunit in Escherichia coli and Their Activity Assay

结果酶切鉴定、SDS-PAGE及westernblot分析证实，成功地构建了pQ-ELP原核非融合表达载体，该载体转化大肠埃希菌在IPTG诱导下能高效表达ELP蛋白。

Results Restriction endonuclease analysis , SDS-PAGE and Western blot proved that a construct expressing non-fused ELP protein was successfully established . When the recombinant plasmid was transformed into E. coli and induced with IPTG , it could efficiently express ELP protein .

目的：制备人类8型疱疹病毒（HHV-8）K8.1N基因编码包膜糖蛋白的原核表达融合蛋白，并鉴定其抗原特异性。

Objective : To express the envelope glycoprotein K8.1N coding gene of human herpesvirus 8 ( HHV-8 ) in E. coli , and further identify its antigenic specification .

方法在建立了多房棘球绦虫elp基因克隆的基础上，应用亚克隆方法将目的基因插入原核非融合表达载体pQE30（+）。

Methods Based on the successful cloning of elp gene of E. multilocularis and subcloning technique , the target elp gene was inserted into a prokaryotic non-fusion expression vector pQE30 ( + ) .

原核表达融合蛋白的亲和层析法纯化

Affinity purification of the tropic 1808 gene fusion protein by pronucleus expression

原核表达融合型血管生成抑制剂Kringle5发酵条件的优化和初步纯化

Optimization of Batch Fermentation and Preliminary Purification for Fusion Angiogenesis Inhibitor Kringle 5 in Prokaryotic System

westernblot法显示，9株单抗均能特异性识别原核表达K8.1/GST融合蛋白和BCBL-1中KSHVK8.1包膜糖蛋白。结论：成功制备了KSHV包膜糖蛋白K8.1单克隆抗体。

Western blot analysis demonstrated that McAbs produced by nine cell lines could specifically recognize the prokaryotic expressed fusion protein K8.1/GST and the envelope glycoprotein K8.1 of KSHV in BCBL-1.Conclusion : McAbs against the envelope glycoprotein K8.1 of KSHV were prepared successfully .

两种血吸虫病疫苗候选分子在原核细胞的融合表达

The fusion expression of two candidate of Schistosoma japonicum vaccine in prokaryotic cell

人乳铁蛋白在原核中的融合表达

Cloning and fusion expression of human lactoferrin protein gene in prokaryotic expression vector

在原核系统中融合表达得到相对分子质量约31000的融合蛋白，占菌体总蛋白的21%。

The ratio of Tat fusion protein to total bacteria proteins was 21 % .

结论：改良的人源性LL37多肽以原核细胞进行融合表达是可行的，并具有较强的杀菌活性。

CONCLUSION : It is possible that the rLL-37 is expressed in procaryotic cell by fusion and it possesses a strong bactericidal activity .

半胱氨酸对原核表达的pS2融合蛋白复性的影响

The effect of cysteine on the renaturation of denatured pS2 fusion protein expressed in prokaryote

构建p38Loop12（L12）的TAT融合表达载体，纯化原核表达的p38L12融合蛋白并鉴定其在真核细胞内的功能。

A prokaryotic expression vector p38 Loop-12 fused with HIV-1 TAT sequence was constructed for the expression and purification of the fusion proteins for cellular transduction and functional identification in eukaryotic cell .

方法：采用蛋白质计算机分析软件预测α-胞衬蛋白的抗原决定簇，设计8条重叠蛋白片段序列，应用GST融合表达系统原核表达该系列融合蛋白。

Methods : Based on the sequence of α - fodrin , antigenic determinants of α - fodrin was predicted by using computer analysis . Eight overlapping protein segments containing antigenic epitopes of α - fodrin were expressed by GST fusion protein expression system .

Tα1在原核细胞中的融合表达及活性研究

Fusion Expression and Activity Testing of Thymosin α 1 in Prokaryotic Cells

同时对原核表达体系以及融合蛋白的表达特性进行了优化与分析。

The prokaryotic expression system was also optimized .

为了证明实验获得的EF-Tu蛋白具有免疫原性，利用原核载体表达重组融合蛋白EF-Tu-His，采用Ni-NTA亲和层析柱对该融合蛋白进行了纯化，用质谱进行鉴定，然后制备兔多克隆抗体。

Second , in order to prove that protein EF-Tu we acquired had immunogenicity , we expressed the recombination protein EF-Tu-His by prokaryotic expression system , and purified it with Ni-NTA chelating affinity chromatography , identified by mass spectrum and prepared rabbit polyclonal antibody also .