Expression and purification of recombinant immunotoxin—a fusion protein stabilizes a single-chain Fv (scFv) in denaturing condition
- 12 December 2002
- journal article
- Published by Elsevier BV in Protein Expression and Purification
- Vol. 27 (1), 85-89
- https://doi.org/10.1016/s1046-5928(02)00539-9
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Characterization of Monoclonal Antibodies Against Carcinoembryonic Antigen (CEA) and Expression inE. coliHybridoma, 2001
- Recombinant immunotoxins: protein engineering for cancer therapyMolecular Medicine Today, 1996
- Clinical evaluation of tumor targeting with the anticarcinoembryonic antigen murine monoclonal antibody fragment, MN-14 F(ab)2Cancer, 1996
- Tumor localization of anti-CEA single-chain Fvs: improved targeting by non-covalent dimersImmunotechnology, 1996
- Expression studies of catalytic antibodies.Proceedings of the National Academy of Sciences of the United States of America, 1995
- Production of stable anti-digoxin Fv in escherichia coliMolecular Immunology, 1992
- A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodiesAnalytical Biochemistry, 1992
- Monoclonal Antibodies in Diagnosis and TherapyScience, 1991
- Functional domains of pseudomonas exotoxin identified by deletion analysis of the gene expressed in E. coliCell, 1987
- Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution.Proceedings of the National Academy of Sciences of the United States of America, 1986