Use of Ubp1 protease analog to produce recombinant human growth hormone in

Use of Ubp1 protease analog to produce recombinant human growth hormone in Escherichia coli

BACKGROUND Numerous bacterial human growth hormone (hGH) expression methods under conventional fermentation and induction conditions have been described. Despite significant progress made in this area over the past several years, production of recombinant hGH by using cellular expression systems still requires further optimization. Fusion of the ubiquitin (Ub) tag to the hGH protein allowed to ...

Transformation and gene expression study of recombinant fish GnRH in E. coli BL21 in order to produce recombinant hormone

Gonadotropin releasing hormone (GnRH) is a neuropeptide known to regulate reproduction in vertebrates. Different analogues of synthetic GnRH are used to induce final sexual maturation in fish breeders. The purpose of this research was to evaluate the expression of recombinant GnRH (rGnRH) in Escherichia coli BL21 to produce recombinant hormone. In the present research, the sequence of DNA relat...

Evaluation of Heat Induction Strategy for Recombinant Human Growth Hormone Expression in Fed-Batch Fermentation

Purification of Large Quantities of Biologically Active Recombinant Human Growth Hormone

Production and purification of human growth hormone using a simple method was studied in two recombinantEscherichia coli, D7-5 and C27-2 strains. The r-hGH was expressed in the form of inclusion body in a batchfermentation process and purified to 99% purity using a procedure based on acid precipitation of the hostderived proteins and other impurities. The effect of the pH and ...

An ln vivo Assay for Biological Activity of Synthesized Recombinant Human Growth Hormone