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RISS 인기검색어
- 검색키워드
- 저자 : 원영한 (검색결과 1 건)
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Escherichia coli is one of the most widely used hosts for the production of heterologous proteins because of its ability to grow rapidly and at high density on inexpensive substrates, its well-characterized genetics and the availability of an increasingly large number of cloning vectors and mutant host strains. But all proteins are not soluble in E.coli. The protein structural study through the crystallization of human-derived protein has some difficulty with over expression of huge amount of human-derived protein in E.coli. In order to overcome the difficulties affecting protein over expression, the variety changes of expression condition, such as temperature, media type, IPTG concentration, heat shock, cold shock, were given systematically for checking the solubilization of the non-soluble proteins to the target protein expression batch. By this systematic method, some proteins such as 14-3-3, Exportin 6, Topoisomerase V, SIRT1(241-356), SIRT2(34-356), SIRT2(50-356) could be expressed in a large amount which is sufficient for the crystallization of the protein although the expression conditions of each protein was different repectively. These results suggest a hint for the overexpression of the non-soluble protein.
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