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Expression and purification of EBV-LMP2 protein / 中华实验和临床病毒学杂志
Chinese Journal of Experimental and Clinical Virology ; (6): 168-170, 2010.
Article in Chinese | WPRIM | ID: wpr-316934
ABSTRACT
<p><b>OBJECTIVE</b>To obtain a second Epstein-Barr virus membrane protein (LMP2) in insect cells.</p><p><b>METHODS</b>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.</p><p><b>RESULTS</b>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.</p><p><b>CONCLUSION</b>The EBV-LMP2 was expressed in insect cells, and the purified LMP2 protein was obtained.</p>
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Virulence / Recombinant Proteins / Viral Matrix Proteins / Blotting, Western / Baculoviridae / Herpesvirus 4, Human / Cell Biology / Electrophoresis, Polyacrylamide Gel / Genetic Vectors / Genetics Limits: Animals Language: Chinese Journal: Chinese Journal of Experimental and Clinical Virology Year: 2010 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Virulence / Recombinant Proteins / Viral Matrix Proteins / Blotting, Western / Baculoviridae / Herpesvirus 4, Human / Cell Biology / Electrophoresis, Polyacrylamide Gel / Genetic Vectors / Genetics Limits: Animals Language: Chinese Journal: Chinese Journal of Experimental and Clinical Virology Year: 2010 Type: Article