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Protein Sci. 2008 Dec;17(12):2120-6. doi: 10.1110/ps.038299.108. Epub 2008 Sep 11.

Novel affinity tag system using structurally defined antibody-tag interaction: application to single-step protein purification.

Author information

1
Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.

Abstract

Biologically important human proteins often require mammalian cell expression for structural studies, presenting technical and economical problems in the production/purification processes. We introduce a novel affinity peptide tagging system that uses a low affinity anti-peptide monoclonal antibody. Concatenation of the short recognition sequence enabled the successful engineering of an 18-residue affinity tag with ideal solution binding kinetics, providing a low-cost purification means when combined with nondenaturing elution by water-miscible organic solvents. Three-dimensional information provides a firm structural basis for the antibody-peptide interaction, opening opportunities for further improvements/modifications.

PMID:
18787202
PMCID:
PMC2590912
DOI:
10.1110/ps.038299.108
[Indexed for MEDLINE]
Free PMC Article

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