2010•PubMedRequires access

[Expression and purification of EBV-LMP2 protein].

Zhan Wang, Jing Ma, Ling Zhou, Xiaoguang Zhang, Haijun Du, Song-Mei Yang, Yi Zeng

Abstract

OBJECTIVE: To obtain a second Epstein-Barr virus membrane protein (LMP2) in insect cells. METHODS: The full length EBV-LMP2 gene was inserted into baculovirus expression transfer vector pFastBac HT B to obtain the recombinant baculoviruses Bac-LMP2. And generation of recombinant baculoviruses was followed by transfection of the recombinant Bac-LMP2 into insect cells, then the recombinant LMP2 protein was recognized by SDS-PAGE and western blot. The expressed LMP2 protein was purified by one step with Ni-NTA metal chelation chromatography. RESULTS: The expressed LMP2 protein was confirmed by SDS-PAGE and western blot. The purity of purified LMP2 protein is up to 86% by HPLC analysis. CONCLUSION: The EBV-LMP2 was expressed in insect cells, and the purified LMP2 protein was obtained.

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Key concepts: Recombinant DNA, Western blot, Molecular biology, Virology, Gene, Affinity chromatography, Biology, Transfection