Endo-β-Galactosidase, Bacteroi
des fragilis, Recombinant, E. coli，Endo-β-Galactosidase, Bacteroides fragilis, Recombinant, <i>E. coli</i>, hydrolyzes internal β-galactosidic linkages of oligosaccharides in poly-N-acetyl-lactosamine structures.，阿拉丁- ￥4867.90
- 阿拉丁
- 上海
- E755034
- 2025年07月11日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
2-8°C储存
- 英文名：
Endo-β-Galactosidase, Bacteroides fragilis, Recombinant, E. coli
- 库存：
期货
- 供应商：
上海阿拉丁生化科技股份有限公司
- 规格：
E755034-50μl
Recombinant, Bacteroides fragilis endo-β-galactosidase expressed in E. coli. Endo-β-Galactosidase is an enzyme that hydrolyzes internal β-galactosidic linkages of oligosaccharides in poly-N-acetyl-lactosamine structures. This enzyme resembles the Escherichia freundii enzyme due to its specificity towards bovine corneal keratan sulphate, milk oligosaccharides and the glycolipids lacto-N-neotetraosylceramide and lacto-N-tetraosylceramide.Recombinant, Bacteroides fragilis endo-β-galactosidase expressed in E. coli. Endo-β-Galactosidase is an enzyme that hydrolyzes internal β-galactosidic linkages of oligosaccharides in poly-N-acetyl-lactosamine structures. This enzyme resembles the Escherichia freundii enzyme due to its specificity towards bovine corneal keratan sulphate, milk oligosaccharides and the glycolipids lacto-N-neotetraosylceramide and lacto-N-tetraosylceramide. Optimum pH: 5.8.
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文献和实验Expression and Preparation of Fusion Proteins from Recombinant gt1.1 Phages
-level expression, the relative stability of β-galactosidase fusion proteins, and simple approaches to purify the fusion proteins. After the desired clone is detected and purified, it is often necessary to obtain preparative amounts of recombinant protein
Expression and Preparation of Fusion Proteins from Recombinant gt11 Phages
by the fusion of the foreign sequence to the carboxyl-terminus of β-galactosidase in λgt11 expression system. The conventional method for preparing fusion proteins from the recombinant λgt11 clones involves production of phage lysogens in Escherichia coli strain
The Generation of Multicopy Recombinant Strains
. Some of the earliest studies supported this strategy, e.g., expression of β-galactosidase or hepatitis B surface antigen was efficient and was not improved by increasing vector copy number (1 ,2 ).
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