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Updated: May 11, 2026
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
[The expression, purification and characterization of β-hCG protein in E.coli]
Wei Wang1, Xiaotao Yin, Yunqi Li
1Department of Urology, General Hospital of PLA, Beijing 100853, China. wayewong261@yahoo.cn
Objective:
To obtain β-chain human chorionic gonadotropin (β-hCG) fusion protein (β-hCG/GST) and identify its antigenicity.
Methods:
The full-length gene of β-hCG was amplified by PCR. The PCR product was cloned into pET-42a prokaryotic expression vector to construct the recombinant plasmid pET-42a-β-hCG, and then it was transformed into BL21 (DE3) for β-hCG/GST fusion protein expression under IPTG induction. After SDS-PAGE assay, the fusion protein was purified by affinity chromatography and identified by Western blotting. The antigenicity of the purified fusion protein was characterized by ELISA.
Results:
The β-hCG gene we obtained had an identical sequence to that retrieved in GenBank. The prokaryotic expression vector pET-42a-β-hCG was successfully constructed as confirmed by enzyme digestion and DNA sequencing. Both Western blotting and ELISA demonstrated that the purified β-hCG fusion protein had satisfactory antigenicity.
Conclusion:
The purified β-hCG/GST fusion protein with satisfactory antigenicity has been obtained, which will facilitate further study on active anti-tumor immunotherapy targeting β-hCG.
