1.
Chinese Journal of Immunology
;
(12): 1119-1121, 2009.
Artigo
em Chinês
| WPRIM
| ID: wpr-403564
RESUMO
Objective:To prepare and purify recombinant human zona pellucida 3 protein,and to study its immunologic activity.Methods:The E.coli BL21 containing recombinant plasmid pGEX4T-1/ huZP3 was induced to express GST-fusion protein by IPTG.After a series of purification procedure,the purified protein was analyzed by SDS-PAGE.After the mice immunized with rhuZP3,the antibody responses against rhuZP3 were detected by ELISA.Results:The soluble fusion protein was expressed,and purity of rhuZP3 was 95%.Moreover, purity of rhuZP3 could be recognized by anti-human ZP3 in ELISA.Conclusion:The rhuZP3 is obtained through the preparation of prokaryotic expression system and anti-rhuZP3 antibody has immunological activity.