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- Title
Cloning, expression, purification, antiserum preparation and its characteristics of the truncated UL6 protein of herpes simplex virus 1.
- Authors
Li, Meili; Cui, Wei; Mo, Chuncong; Wang, Jinlin; Zhao, Zhiyao; Cai, Mingsheng
- Abstract
The herpes simplex virus 1 (HSV-1) portal protein UL6 is important for HSV-1 replication, however, its precise functions in the virus life cycle are poorly understood. As we known, a relatively important tool for disclosing these functions is the antiserum specifically detecting UL6 in the HSV-1-infected cell. To this end, a recombinant protein consisting of C-terminal 297-676 amino acids of UL6 fused to His-tag was expressed in E. coli and purified from inclusion body by the Ni-NTA affinity chromatography under denaturing conditions, which was then refolded and used for the preparation of antiserum in rabbit. As results, western blot and immunofluorescence assay showed that this antiserum could specifically detect the purified truncated UL6 as well as native UL6 in the HSV-1 infected cells, indicating that the prepared antiserum could serve as a valuable tool for further exploring the functions of UL6.
- Subjects
HERPES simplex virus; IMMUNE serums; RECOMBINANT proteins; CLONING; GENE expression; MOLECULAR cloning; WESTERN immunoblotting
- Publication
Molecular Biology Reports, 2014, Vol 41, Issue 9, p5997
- ISSN
0301-4851
- Publication type
Article
- DOI
10.1007/s11033-014-3477-y