[Expression and purification of EBV-LMP2 protein].

Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi

State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China.

Published: June 2010

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Article 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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