الفهرس 
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Abstract
The present study aimed to express the recombinant human interleukin-2 (IL2) protein in considerable amounts that could be used as a positive control for early diagnosis of tumors or in cancer research in Egypt. Another aim was to investigate the effect of different expression conditions on the solubility behavior of eukaryotic protein expressed in E. coli. To fulfill this aim, two versions of synthetic sequence of the cDNA encoding IL2 protein were incorporated into pRSET-B vector. The first version produced N-terminal his-tagged mature IL2 protein while the second version produced N- and C-terminal his-tagged mature IL2 protein as atrial to increase the solubility. Besides, the expression was carried out under different conditions to avoid formation of IBs: Decreasing incubation temperature, decreasing IPTG concentration, and earlier harvesting. Moreover, we investigated different lysis methods that include either mechanical or enzymatic lysis or both together. Then, the expressed IL2 protein was purified from IBs via Metal Ion affinity chromatography. A simple protocol was optimized for the solubilization of IBs of the two His-tagged recombinant proteins depending on washing of the IBs with low concentrations of tritone and urea to get rid of cell wall and cell membrane components. The guanidine hydrochloride was used for solubilization of the IBs. The yield for His-IL2 and His-IL2-His proteins was found to be 5.1 mg and 4.5 mg/cell pellet of 1L culture respectively as determined by Bradford assay method.