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Acta Virologica Vol.54, No.2, p.147-150, 2010 |
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Title: Recombinant N-terminal part of Bovine herpesviru 1 ICP27 protein: its preparation, purification, and use for raising specific antiserum | ||
Author: L. Zhao, X. Ren, H. Guo, Q. Ding, A. C. Zheng | ||
Abstract: Recombinant N-terminal part of bovine herpesvirus-1 (BoHV-1) ICP27 protein fused with thioredoxin and His-tag (“the recombinant protein”) expressed in Escherichia coli was purified by the Ni2+-NTA affinity chromatography and used for the preparation of antiserum by immunization of rabbits. The antiserum recognized the recombinant protein in Western blot analysis and was able to detect BoHV-1 ICP27 in the nucleoli of BoHV-1-infected MDBK cells. These results showed that such an antiserum could serve as a valuable tool in further studies of the functions of BoHV-1 ICP27. |
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Keywords: Bovine herpesvirus 1, ICP27, recombinant protein, antiserum, immunofluorescence assay | ||
Year: 2010, Volume: 54, Issue: 2 | Page From: 147, Page To: 150 | |
doi:10.4149/av_2010_02_147 |
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