重组DNA
大肠杆菌
融合蛋白
蛋白质表达
计算生物学
生物
生物化学
细胞生物学
基因
作者
Yoav Peleg,Tamar Unger
出处
期刊:Methods in molecular biology
日期:2011-08-31
卷期号:: 173-186
被引量:20
标识
DOI:10.1007/978-1-61779-349-3_12
摘要
Escherichia coli is widely used as an expression system for production of recombinant proteins of prokaryotic and eukaryotic origin. A large body of knowledge has accumulated throughout the last few decades regarding expression of recombinant proteins in E. coli. However, despite this progress, protein production, primarily of eukaryotic origin, still remains a challenge. The biggest obstacle lies in obtaining large amounts of a given protein in a correctly folded form. Several strategies are being used to increase both yield and solubility. These include expression as fusion proteins, co-expression with molecular chaperones, or with a protein partner(s), and the use of multiple constructs for each protein. In this chapter, we focus on strategies for creating expression vectors, as well as on guidelines for improving recombinant protein solubility.
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