Abstract：Gene UL48 of Marek’s disease virus(MDV), encoding the homologue of Herpes simplex virus (HSV) tegument protein VP16, was cloned into pET-32a to obtain pET-VP16. The recombinant vector pET-VP16 was transformed into Escherichia.coli BL21 and solubly expressed in LB medium as a fused protein of about 67 kD with induction of IPTG. And the fusion protein was purified by His·Bind chromatography column. Then immunization in rabbits with the fusion protein was used to obtain the high titer antibody against MDV VP16. Indirect ELISA indicated that the highest titer was over 2×10-5. Moreover, Western blotting analysis proved that the antibody was specific to VP16.
[J]. , 2006, 14(4): 530-534.
QIUYa-feng;GEFei-fei;FENGXiu-li;CHENPu-yan. Fusion Expression and Purification of Marek’s disease virus Tegument Protein VP16 and Its Antibody Preparation. , 2006, 14(4): 530-534.
