Prokaryotic expression of antibodies
- 1 December 2005
- journal article
- review article
- Published by Springer Nature in Cancer and Metastasis Reviews
- Vol. 24 (4) , 501-519
- https://doi.org/10.1007/s10555-005-6193-1
Abstract
Maximizing the expression yields of recombinant whole antibodies and antibody fragments such as Fabs, single-chain Fvs and single-domain antibodies is highly desirable since it leads to lower production costs. Various eukaryotic and prokaryotic expression systems have been exploited to accommodate antibody expression but Escherichia coli systems have enjoyed popularity, in particular with respect to antibody fragments, because of their low cost and convenience. In many instances, product yields have been less than adequate and intrinsic and extrinsic variables have been investigated in an effort to improve yields. This review deals with various aspects of antibody expression in E. coli with a particular focus on single-domain antibodies.Keywords
This publication has 190 references indexed in Scilit:
- A Pentavalent Single-domain Antibody Approach to Tumor Antigen Discovery and the Development of Novel Proteomics ReagentsJournal of Molecular Biology, 2004
- Contributions of CDR3 to VHH Domain Stability and the Design of Monobody Scaffolds for Naive Antibody LibrariesJournal of Molecular Biology, 2003
- Production of Functional Single-Chain Fv Antibodies in the Cytoplasm of Escherichia coliJournal of Molecular Biology, 2002
- Efficient tumor targeting by single‐domain antibody fragments of camelsInternational Journal of Cancer, 2002
- Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies 1 1Edited by R. HuberJournal of Molecular Biology, 2001
- Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?Journal of Molecular Biology, 2000
- Intrabody construction and expression. I. The critical role of VL domain stabilityJournal of Molecular Biology, 1999
- Antibody scFv fragments without disulfide bonds, made by molecular evolution 1 1Edited by I. A. WilsonJournal of Molecular Biology, 1998
- Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coliGene, 1994
- Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coliNature, 1989