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논문 기본 정보

자료유형
학술대회자료
저자정보
You, Je-Kyung (College of Pharmacy, Seoul National University) Shin, Chan-Young (College of Pharmacy, Seoul National University) Park, Kyu-Hwan (College of Pharmacy, Seoul National University) Ko, Kwang-Ho (College of Pharmacy, Seoul National University)
저널정보
한국응용약물학회 한국응용약물학회 춘계학술발표논문집 한국응용약물학회 1997년도 춘계학술대회
발행연도
1997.1
수록면
93 - 93 (1page)

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Analysis of protein is often frustrated by the inability to isolate large amounts of purified protein from a native source. To overcome this problem, fusion protein expression systems such as pGEX system have been widely used. Using pGEX system, the desired protein could be easily obtained in a large amount in E. coli, and then the fusion protein could be used for the study of the function of the given protein. To analyze and purify the GST fusion protein, anti-GST antibody could be used as one of the system of choice. However, the production and characterization of monoclonal anti-GST antibody has not been studied extensively yet. To produce monoclonal anti-GST antibody, GST was purified from E. coli transformed with pGEX-cs, one of the pGEX system and was used as an antigen. The monoclonal antibody was produced by fusion of the immunized spleen cells with SP2-0 myeloma cells. The antibody was characterized by ELISA, western blotting, etc. The monoclonal antibody produced in this study (mAb-GSTA) showed strong and specific immunoreactivity against not only GST but also GST-fusion proteins. Also, mAb-GSTA was successfully used for the immunoaffinity purification of the GST ${\beta}$-Rc.-third intracellular-loop fusion protein. The results of the present study suggest that mAb-GSTA may be used for the identification and purification of GST fusion proteins.

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