Related Experiment Video
Updated: Sep 15, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
Immobilization of monoclonal antibodies for affinity chromatography using a chelating peptide
P Loetscher1, L Mottlau, E Hochuli
1F. Hoffmann-La Roche Ltd., Pharma Research, New Technologies, Basle, Switzerland.
Abstract:
A procedure was developed for oriented immobilization of monoclonal antibodies on a solid support. The technique involves the specific oligosaccharide-directed covalent modification of the monoclonal antibody (mAb) with the chelating peptide, Lys-Gly-(His)6, in conjunction with immobilized metal ion affinity chromatography. Chelating peptide-mAb conjugates with a molar ratio of 2.2 retained full antigen binding activity. On immobilization of the modified antibodies on a nickel affinity resin, the molar antigen binding ratio was 1.4. The high antigen binding capacity is indicative of oriented immobilization providing maximum access for the antigen. The described method can be used for the preparation of high-capacity immunosorbents for affinity chromatography and it is applicable for all immunoglobulin classes.
More Related Videos
10:33Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
07:53Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study
Published on: August 16, 2019
Related Concept Videos
Hybridoma Technology
Hybridoma Selection
Commonly used fusion techniques — electroporation, polyethylene glycol...
Immunoprecipitation
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Affinity Chromatography