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Direct Immunoprecipitation of Antigen with Phage Displaying Immunoglobulin Fragment
Author(s) -
Pieter Telleman,
Gillian A. Kingsbury,
Richard P. Junghans
Publication year - 2000
Publication title -
biotechniques
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.617
H-Index - 131
eISSN - 1940-9818
pISSN - 0736-6205
DOI - 10.2144/00296st04
Subject(s) - bacteriophage , antigen , immunoprecipitation , phage display , antibody , biology , phagemid , microbiology and biotechnology , chemistry , virology , biochemistry , escherichia coli , genetics , gene
Phage libraries may display hormones, receptors, antibody fragments, etc., by fusion to phage envelope proteins. This report describes the direct precipitation of phage-Fab-antigen complexes by polyethylene glycol precipitation, resulting in highly selective and efficient recovery of antigen from complex mixtures without nonspecific protein contamination. The method demonstrates efficiency and specific recovery of phage-Fab-antigen complexes from a background of a complex mixture of unrelated proteins as may occur in the analysis of biological specimens. This simple, fast, and effective method allows isolation and characterization of target antigens, with no need to further process Fab or sFv, and may reasonably be extended to isolate any interacting partner molecule for any displayed protein.

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