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rhTum5融合蛋白的克隆、表达、纯化及鉴定
http://www.100md.com 《第四军医大学学报》 2005年第14期
pQE载体,,Tumstatin;,Tum5;,蛋白纯化;pQE载体,0引言,1材料和方法,2结果,3讨论,【参考文献】
     Identification, purification, expression and cloning of fusion protein rhTum5

    MA Nan, ZHANG YingQi, YAN Zhen

    Biotechnology Center, the Fourth Military Medical University, Xian 710033, China

    【Abstract】 AIM: To construct the recombinant expression vector of Tum5 and to purify,identify the fusion protein rhTum5. METHODS: A 264bp of human Tum5 gene fragment was synthesized and cloned into pQE30 vector,an E.coli expression vector.The plasmid was transformed into E.coli DH5α and induced to express fusion protein rhTum5 with IPTG..The expression of Tum5 was detected by TricineSDSPAGE and Western blot. RESULTST:A novel protein with expected molecular mass was expressed upon induction with IPTG. Expressed product accounted for about 40% of total bacterial proteins and the expressed product showed good reactivity to antiHis tag antibody. CONCLUSION: Our successful cloning and expression of human Tum5 gene and purification of rhTum5 protein lay a basis for further study on the application of this protein to antiangiogenesis in vitro and in vivo. ......

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