Cloning and Expression of Recombinant Human Growth Hormone in E. coli: High-Yield Production and Biological Activity Assessment

Theodor Bilharz Research Institute

Bibliographic Information

Authors: Adly M.A.; Okasha H.; Elwahy A.H.M.; Sabet S.; Nasr S.M.

Journal: Egyptian Journal of Medical Microbiology (Egypt)

Publisher: Egyptian Society for Medical Microbiology (ESMM)

Publication Date: 1 October 2025

Volume / Issue: Volume 34 / Issue 4

Pages: 529–540

ISSN: 11102179

DOI: 10.21608/ejmm.2025.384975.1641

Scopus: View on Scopus

Document Type: Article

Authors and Affiliations

Adly M.A., Biotechnology Department, Faculty of Science, Cairo University, Egypt; Okasha H., Biochemistry and Molecular Biology Department, Theodor Bilharz Research Institute, Giza, Egypt; Elwahy A.H.M., Faculty of Science, Cairo University, Egypt; Sabet S., Department of Zoology, Faculty of Science, Cairo University, Egypt; Nasr S.M., Department of Biochemistry and Molecular Biology, Theodor Bilharz Research Institute, Giza, Egypt

Abstract

Background: The Human Growth Hormone (HGH) is a pituitary gland secretion hormone that stimulates cell division, growth, and repair in humans and animals. It Fis a protein with a molecular weight (MW) equal to 22 kDa. Objectives: Production of HGH in prokaryotic expression system via synthetic gene coding design for HGH. Methodology: Cloning the HGH-designed coding sequence in a pET-3a expression vector for protein synthesis in BL21 DE3 E. coli strain. The expressed recombinant HGH (rHGH) at the batch fermentation level was purified according to HGH MW and its biological activity was assayed. Results: 24 h batch fermentation showed a bacterial growth at OD595 equal to 1.6 ± 0.023 and the wet cell weight (WCW) was 16.4 ± 0.32 gm/L. Immunodetection confirmation of rHGH using Western blot showed a 22 kDa band at the expected MW. Purification of HGH using anion exchange chromatography revealed a concentration of purified rHGH of about 480.22 µg/ml. Using normal Vero cells, the activity of purified rHGH was 0.228 IU/mg. Conclusion: Native rHGH protein was produced at a large scale with potential biological activity compared to standard HGH; somatotropin, using modern technologies in recombinant DNA. © 2025, Egyptian Society for Medical Microbiology (ESMM). All rights reserved.

Keywords

Activity assay; Cloning; E. coli; HGH; Protein purification; Western Blot

Citation Information

Scopus Citations: 0

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