High-level soluble expression of hIGF-1 fusion protein in recombinant Escherichia coli
β Scribed by Danping Zhang; Peilian Wei; Limei Fan; Jiazhang Lian; Lei Huang; Jin Cai; Zhinan Xu
- Book ID
- 108254773
- Publisher
- Elsevier Science
- Year
- 2010
- Tongue
- English
- Weight
- 460 KB
- Volume
- 45
- Category
- Article
- ISSN
- 1873-3298
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Three native E. coli proteins-NusA, GrpE, and bacterioferritin (BFR)-were studied in fusion proteins expressed in E. coli for their ability to confer solubility on a target insoluble protein at the C-terminus of the fusion protein. These three proteins were chosen based on their favorable cytoplasmi
Producing soluble proteins in __Escherichia coli__ is still a major bottleneck for structural proteomics. Therefore, screening for soluble expression on a small scale is an attractive way of identifying constructs that are likely to be amenable to structural analysis. A variety of expression-screeni
## Abstract Extracellular production of recombinant proteins in __Escherichia coli__ has several advantages over cytoplasmic or periplasmic production. However, nonpathogenic laboratory strains of __E. coli__ generally excrete only trace amounts of proteins into the culture medium under normal grow