Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies
- 14 March 2002
- journal article
- Published by Elsevier in Journal of Immunological Methods
- Vol. 263 (1-2), 133-147
- https://doi.org/10.1016/s0022-1759(02)00036-4
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- High Resolution Mapping of the Binding Site on Human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and Design of IgG1 Variants with Improved Binding to the FcγRJournal of Biological Chemistry, 2001
- Recombinant human IgG molecules lacking Fcγ receptor I binding and monocyte triggering activitiesEuropean Journal of Immunology, 1999
- The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regionsMolecular Immunology, 1995
- Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site‐directed mutagenesisEuropean Journal of Immunology, 1994
- Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumour growth in vivoNature, 1993
- Interaction of aglycosyl immunoglobulins with the IgG Fc transport receptor from neonatal rat gut: Comparison of deglycosylation by tunicamycin treatment and genetic engineeringMolecular Immunology, 1992
- Comparative biological properties of a recombinant chimeric anti-carcinoma mAb and a recombinant aglycosylated variantCancer Immunology, Immunotherapy, 1992
- High Level Escherichia coli Expression and Production of a Bivalent Humanized Antibody FragmentNature Biotechnology, 1992
- A structured model for monoclonal antibody synthesis in exponentially growing and stationary phase hybridoma cellsBiotechnology & Bioengineering, 1991
- An Fc receptor structurally related to MHC class I antigensNature, 1989