PURIFICATION AND CHARACTERIZATION OF RECOMBINANT IL-4 AND ANTI-IL-4 ANTIBODY FROM TRANSFECTED CHO CELL LINE AND HYBRIDOMA, RESPECTIVELY

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TAVAKOL AFSHARI J.; GHOLAMZAD M.; ZAMANI ALI REZA

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Journal: Iranian Journal of Basic Medical Sciences Year:2003 | Volume:6 | Issue:3 (19) Page(s): 194-201

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Title

PURIFICATION AND CHARACTERIZATION OF RECOMBINANT IL-4 AND ANTI-IL-4 ANTIBODY FROM TRANSFECTED CHO CELL LINE AND HYBRIDOMA, RESPECTIVELY

Author(s)

TAVAKOL AFSHARI J. | GHOLAMZAD M. | ZAMANI ALI REZA | Issue Writer Certificate

Keywords

INTERLEUKINE-4Q3

T-CELL LINEQ4

CHO CELLQ4

HYBRIDOMAQ4

Abstract

INTERLEUKINE-4 (IL-4) is one of the most important cytokine that secreted by T Iymphocytes. This molecule has variety of effects on hematopoietic cells, especially cells that involve in immune system. IL- 4 gene cloned in various expression vectors such as E.Coli, Yeast and recently mammalian cells. By those ways IL-4 can be expressed and then purified. There is no documented report about the expression of hIL-4 cDNA in mamalian cell line like CHO CELL line. In this study CHO (Chinese Hamster Ovary cells) which had been transfected with IL-4 gene was used as an expression vector. For this purpose, anti-IL-4 monoclonal antibody was prepared by specific HYBRIDOMA. For antibody and rIL-4 recovery, cell culture techniques had been set up. For this purpose, frozen hIL-4 cDNA transfected and HYBRIDOMA cells were thawed and cultured. Culture supernatant was collected. This supernatant of HYBRIDOMA cell culture was processed for antibody recovery by protein A Sepharose and purified antibody was attached to activated Sepharose gel as a ligand for affinity chromatography. Then affinity chromatography method used for rIL-4 purification from CHO CELL culture supernatant. Purified sample was evaluated by SDS-PAGE. By this method one band with molecular weight of about 27KD was appeared. This band was transferred to nitrocellulose membrane and blotted by anti-IL-4 antibody and labeled by HRP conjugated anti-mouse antibody to confirm antigen-antibody complex formation in membrane. Based on our Results, affinity chromatography is the most simple and efficient method for IL-4 purification from culture supernatant contains protein.

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APA: Copy

TAVAKOL AFSHARI, J., GHOLAMZAD, M., & ZAMANI, ALI REZA. (2003). PURIFICATION AND CHARACTERIZATION OF RECOMBINANT IL-4 AND ANTI-IL-4 ANTIBODY FROM TRANSFECTED CHO CELL LINE AND HYBRIDOMA, RESPECTIVELY. IRANIAN JOURNAL OF BASIC MEDICAL SCIENCES, 6(3 (19)), 194-201. SID. https://sid.ir/paper/52386/en

Vancouver: Copy

TAVAKOL AFSHARI J., GHOLAMZAD M., ZAMANI ALI REZA. PURIFICATION AND CHARACTERIZATION OF RECOMBINANT IL-4 AND ANTI-IL-4 ANTIBODY FROM TRANSFECTED CHO CELL LINE AND HYBRIDOMA, RESPECTIVELY. IRANIAN JOURNAL OF BASIC MEDICAL SCIENCES[Internet]. 2003;6(3 (19)):194-201. Available from: https://sid.ir/paper/52386/en

IEEE: Copy

J. TAVAKOL AFSHARI, M. GHOLAMZAD, and ALI REZA ZAMANI, “PURIFICATION AND CHARACTERIZATION OF RECOMBINANT IL-4 AND ANTI-IL-4 ANTIBODY FROM TRANSFECTED CHO CELL LINE AND HYBRIDOMA, RESPECTIVELY,” IRANIAN JOURNAL OF BASIC MEDICAL SCIENCES, vol. 6, no. 3 (19), pp. 194–201, 2003, [Online]. Available: https://sid.ir/paper/52386/en

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