Expression and Purification of the DNA Binding Domain of the Epstein-Barr Virus Nuclear Antigen 1  

Expression and Purification of the DNA Binding Domain of the Epstein-Barr Virus Nuclear Antigen 1

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作  者:Meiru Hu~1 Ru Wei~(1,2)Lu Qian~1 Ming Yu~1 Ming Shi~1 Kun He~3 Jie Wang~3 Beifen Shen~1 Ning Guo~1 (1 Institute of Basic Medical Sciences,Beijing 100850 2 North China Coal Medical College 3 National Center of Biomedical Analysis,Beijing 100071) 

出  处:《生物技术通报》2008年第S1期405-410,共6页Biotechnology Bulletin

基  金:supposed by National Basic Research Program of China(973 Program)(2006CB504305);Beijing Natural Science Foundation(No.7051006).

摘  要:To overexpress EBNA-1 in E.coli and generate the specific antibody,in this study,the antigenicity,epitope and hydrolysis of EBNA-1 were analyzed using the computer design software Biosun.Based on the prediction by computer analysis,the sequence encoding EBNA-1385-557 was amplified by PCR with the specific primers.The expression vector containing EBNA-1385-557 coding sequence was constructed.His-tagged EBNA-1385-557 was expressed in E.coli.The soluble recombinant protein was purified using Ni-NTA chromatography.The purified protein was used as antigens to immunize mice and screen the antibodies,which will serve as an important tool for further studies.To overexpress EBNA-1 in E.coli and generate the specific antibody,in this study,the antigenicity,epitope and hydrolysis of EBNA-1 were analyzed using the computer design software Biosun.Based on the prediction by computer analysis,the sequence encoding EBNA-1385-557 was amplified by PCR with the specific primers.The expression vector containing EBNA-1385-557 coding sequence was constructed.His-tagged EBNA-1385-557 was expressed in E.coli.The soluble recombinant protein was purified using Ni-NTA chromatography.The purified protein was used as antigens to immunize mice and screen the antibodies,which will serve as an important tool for further studies.

关 键 词:EBNA-1 EXPRESSION PURIFICATION E.COLI 

分 类 号:Q939.4[生物学—微生物学] Q78

 

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