High-Level Expression of Soluble Protein inEscherichia coliUsing a His6-Tag and Maltose-Binding-Protein Double-Affinity Fusion System
- 1 August 1997
- journal article
- Published by Elsevier in Protein Expression and Purification
- Vol. 10 (3) , 309-319
- https://doi.org/10.1006/prep.1997.0759
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.Published by Elsevier ,2021
- Structural Studies of Escherichia coli UDP-N-Acetylmuramate:l-Alanine LigaseBiochemistry, 1996
- High-Yield Expression, Refolding, and Purification of Penicillin-Binding Protein 2a from Methicillin-Resistant Staphylococcus aureus Strain 27RProtein Expression and Purification, 1995
- New vectors for high level expression of recombinant proteins in bacteriaAnalytical Biochemistry, 1992
- [6] Use of T7 RNA polymerase to direct expression of cloned genesPublished by Elsevier ,1990
- An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding proteinGene, 1988
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding proteinGene, 1988
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the β-galactosidase structural gene of Escherichia coliJournal of Molecular Biology, 1967