One-Step Purification of Recombinant Proteins Using a Nanomolar-Affinity Streptavidin-Binding Peptide, the SBP-Tag
- 31 December 2001
- journal article
- Published by Elsevier BV in Protein Expression and Purification
- Vol. 23 (3), 440-446
- https://doi.org/10.1006/prep.2001.1515
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- The use of mRNA display to select high-affinity protein-binding peptidesProceedings of the National Academy of Sciences of the United States of America, 2001
- Constructing high complexity synthetic libraries of long ORFs using In Vitro selectionJournal of Molecular Biology, 2000
- Streptavidin-binding and -dimerizing ligands discovered by phage display, topochemistry, and structure-based designBiomolecular Engineering, 1999
- Mutagenesis of a flexible loop in streptavidin leads to higher affinity for the Strep-tag II peptide and improved performance in recombinant protein purification"Protein Engineering, Design and Selection", 1997
- Molecular Interaction Between the Strep-tag Affinity Peptide and its Cognate Target, StreptavidinJournal of Molecular Biology, 1996
- The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment"Protein Engineering, Design and Selection", 1993
- Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus.Proceedings of the National Academy of Sciences of the United States of America, 1991
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product.Molecular and Cellular Biology, 1985
- [75] Maltose-binding protein from Escherichia coliMethods in Enzymology, 1982