Use of Thiophilic Adsorption Chromatography for the One-Step Purification of a Bacterially Produced Antibody Fab Fragment without the Need for an Affinity Tag
- 1 December 1999
- journal article
- research article
- Published by Elsevier in Protein Expression and Purification
- Vol. 17 (3) , 421-427
- https://doi.org/10.1006/prep.1999.1142
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- One-step affinity purification of bacterially produced proteins by means of the “Strep tag” and immobilized recombinant core streptavidinJournal of Chromatography A, 1994
- A general vector, pASK84, for cloning, bacterial production, and single-step purification of antibody Fab fragmentsGene, 1994
- Single-step purification of a bacterially expressed antibody Fv fragment by immobilized metal affinity chromatography in the presence of betaineJournal of Chromatography A, 1993
- Bacterial expression of immunoglobulin fragmentsCurrent Opinion in Immunology, 1993
- Production of stable anti-digoxin Fv in escherichia coliMolecular Immunology, 1992
- High Level Escherichia coli Expression and Production of a Bivalent Humanized Antibody FragmentNature Biotechnology, 1992
- Cloning and expression of the variable regions of mouse myeloma protein MOPC315 in E. coli: Recovery of active FV fragmentsMolecular Immunology, 1992
- Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coliNature, 1989
- Assembly of a Functional Immunoglobulin F v Fragment in Escherichia coliScience, 1988
- An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding proteinCell, 1986