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- Cayman
- 35714-100 μg
- 2025年07月21日
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文献和实验Thioredoxin and Related Proteins as Multifunctional Fusion Tags for Soluble Expression in E. coli
Escherichia coli has traditionally been a popular host for the production of heterologous proteins because of its ease of genetic manipulation and growth. Recombinant proteins produced in E. coli have been useful for a variety of purposes
Protein Modification to Probe Intradynein Interactions and In Vivo Redox State
interactions involving dynein components by chemical cross-linking and a recently developed technique to assess the in vivo redox state of thioredoxin-like proteins that are associated with axonemal dyneins from a wide range of organisms. Finally
Discovery of New Fusion Protein Systems Designed to Enhance Solubility in E. coli
research experience with fusion proteins containing glutathione S-transferase (GST) (3 ), maltose binding protein (MBP) (4 ), and thioredoxin (5 ) has shown that these proteins can improve the expression and solubility of many heterologous proteins
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