The fusion protein had activity of ICL.
目的蛋白具有ICL的活性。
The fusion protein was obtained by purifying protein a.
蛋白a纯化获得电泳纯融合蛋白。
The fusion protein was purified using fermentation strain.
发酵菌株，纯化制备融合蛋白。
Objective: To express and purify the fusion protein of galectin-1.
目的：表达和纯化半乳糖凝集素- 1融合蛋白。
The inhibition ratio of the fusion protein was tested by MTT method.
MTT法检测融合蛋白对黑色素瘤细胞的体外抑制率。
MLR assay indicated that the fusion protein could inhibit the proliferation of t cells.
同时经混合淋巴细胞反应证明该融合蛋白能明显抑制T细胞的活化增殖能力。
The hematopoietic and chemotactic activities of the fusion protein were investigated in vitro.
研究了该融合蛋白在体外的促造血细胞增殖活性和对免疫细胞的趋化活性。
Results the fusion protein expressed in e. coli account for 20% of the total bacterial protein.
结果融合蛋白的表达量占菌体总蛋白的20%。
The portion of the fusion protein accounted for 26% of all the proteins by thin layer gel optical scanning.
薄层凝胶光密度扫描分析结果显示 ，表达的融合蛋白量约占细菌总蛋白的 2 6%。
Besides, the result of agglutination activity assay indicated the fusion protein still presented agglutination activity.
经凝血活性测定表明该融合蛋白具有凝血活性。
We used the best system to cut on the fusion protein, after activity detected the purpose of peptide has no antibacterial activity.
利用最佳体系对融合蛋白进行切割，经过活性检测发现，目的肽没有抑菌活性。
If the fusion protein of VP1 and VP2 that was expressed in E. coli can form neutralizing antigen epitopes, this problem is resolved.
如果大肠杆菌中表达的VP1和VP2融合蛋白也能形成中和抗原表位，则解决了这个问题。
CONCLUSION the fusion protein of the cloned kininogenase gene was highly expressed in E. coli and could be used for the development of its biological products.
结论成功克隆人胰腺组织激肽原酶基因，并高效表达融合蛋白，为进一步开发基因工程药物打下基础。
The results showed that the fusion protein can yield antibodies with high neutralizing activity as well as provide protection against challenge with virulent virus.
结果表明，用此融合蛋白的包涵体免疫豚鼠能诱导产生中和抗体，并对病毒的攻击提供免疫保护。
To construct the recombinant prokaryotic expression vector containing the ESAT-6 gene of Mycobacterium Boris, purification, expression the fusion protein identified.
构建牛结核分枝杆菌esat - 6基因的原核表达载体，诱导表达、纯化并初步鉴定该蛋白。
After dissolution of inclusion bodies in binding buffer containing 8m Urea, the fusion protein was purified with metal affinity chromatography column, high purity protein was achieved.
包涵体蛋白经含8m尿素的结合缓冲液溶解后，用金属亲和层析法进行纯化，获得了高纯度的目的蛋白。
The titer of the antiserum was respectively 1:256 by agarose double-diffusion analysis and it was 1:12800 by indirect ELISA, specific antisera against the fusion protein were prepared.
琼脂糖双向扩散检测显示抗血清的效价1：25 6，间接ELISA测得的效价1：12 800，结果显示获得了融合蛋白的特异性抗血清。
RESULTS: DDR2/EGFP fusion plasmid was successfully constructed. Further analysis also demonstrated that the fusion protein has similar expression and activation pattern with wild type ones.
结果：成功构建了DDR2/EGFP融合表达载体，进一步的分析也证明此融合表达载体能在细胞中正确表达并可以被配体所激活。
The fusion protein has been proved having immunogenicity when detected by Western blot, which demonstrates that it may be useful in the development of porcine pleuropneumonia subunit vaccine.
该融合蛋白的成功表达为猪传染性胸膜肺炎亚单位疫苗的研制奠定了基础。
CONCLUSION: We successfully construct IP-10 fusion protein expressing vector and get the fusion protein with high bioactivity, which provides essential materials for the future studies on IP-10.
结论：成功构建了人ip - 10融合蛋白表达载体，并纯化得到具有活性的IP - 10融合蛋白，为进一步研究IP - 10的功能提供了重要的实验材料。
Conclusion the prokaryotic expression vector of 8r-muc1 core peptide fusion protein has been constructed, and the fusion protein with biological activity has been successfully expressed and purified.
结论：构建了8r - MUC1核心肽融合蛋白原核表达载体并成功表达与纯化出具有生物学活性的融合蛋白。
Specific antibody was screened by 3 rounds of panning of phage antibody library with the fusion protein. The antigen binding activity and DNA sequences of positive clones were determined and analyzed.
以该融合蛋白为固相抗原，对噬菌体抗体库进行3轮淘筛，并对所获阳性克隆进行抗原结合活性测定和DNA序列测定。
The paper describes process of recombinant fusion protein in purification and existing problems.
本文论述了基因重组融合蛋白纯化过程和存在的问题。
A new medicine in development for the wet form of AMD is a recombinant fusion protein that binds to the growth factor protein that plays a critical role in blood-vessel formation in the eye.
一种在研治疗湿性amd的新药是一种重组融合蛋白，它能结合眼内血管形成关键生长因子蛋白。
Conclusion The GRA7 gene may be expressed as a GST fusion protein in E. coli.
结论GRA7基因在大肠埃希菌中以gst融合蛋白的形式得到表达。
The purity of fusion protein was about 70% after ultrasonic decomposition and washing repeatedly, and reached above 95 % after purification by ion exchange and gel-filtration chromatography.
菌体经过超声破碎后反复洗涤包涵体，融合蛋白纯度达到70%，进一步用离子交换层析和凝胶过滤层析纯化使其纯度达95%以上。
Results: The CAT gene was cloned correctly and it's fusion protein was expressed in E.
结果：成功克隆了CAT的基因片段，并在大肠杆菌中得到其融合蛋白的表达。
Results: The CAT gene was cloned correctly and it's fusion protein was expressed in E.
结果：成功克隆了CAT的基因片段，并在大肠杆菌中得到其融合蛋白的表达。
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