Expression of the rat growth hormone-releasing hormone gene in placenta is directed by an alternative promoter.

P-66: Optimization of Human Luteinizing Hormone Expression in CHO Cells Culture by Stepwise Reduction in Serum Concentration

Background: Mammalian Cell lines are the main expression system for the production of recombinant therapeutic proteins. Optimization of cell culture condition is performed via alteration in different parameter. Cell culture media plays an important role in cell cycle because of compounds such as amino acids, vitamins, inorganic salts, glucose, and serum as a source of growth factors, trace elem...

CONSTRUCTION OF RECOMBINANT PLASMIDS FOR PERIPLASMIC EXPRESSION OF HUMAN GROWTH HORMONE IN ESCHERICHIA COLI UNDER T7 AND LAC PROMOTERS

In order to study the periplasmic expression of human growth hormone (hGH) in Escherichia coli, the related cDNA was inserted in two expression plasmids carrying pelB signal peptide, one with lac bacterial promoter and the other with a bacteriophage T7-based promoter. The recombinant plasmids were moved to TG1 and BL21 strains of E. coli, respectively. To induce the expression systems, IPTG and...

Comparison of Expression of Growth Hormone-Releasing Hormone and Its Receptor Splice Variant 1 in Different Stages of Endometriosis

Comparing The Effects of Glycyrrhiza glabra Root Extract, A Cyclooxygenase-2 Inhibitor (Celecoxib) and A Gonadotropin-Releasing Hormone Analog (Diphereline) In A Rat Model of Endometriosis

Objective The purpose of this study was to compare the effects of Glycyrrhiza glabra (Licorice), Cyclooxygenase-2 Inhibitor (Celecoxib®) and gonadotropin releasing hormone analog (Diphereline®) to a control group on endometrial implants in rats. MaterialsAndMethods Endometriosis was induced in rats by auto transplantation and after confirmation, the rats were divided into 4 groups that were tre...

The Over-Expression of Biologically Active Human Growth Hormone in a T5-Based System in Escherichia coli, Studying Temperature Effect

We studied the expression of human growth hormone (hGH) in E. coli under a bacteriophage T5-base promoter in a pQE30 expression vector. For an efficient expression of hGH cDNA, a number of codons at the hGH N-terminal coding region were altered based on the E. coli major codons. An over-expression of hGH in the bacteria, carrying the recombinant plasmids, was observed at 37°C in the presence of...