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

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.

SUBMITTER: Nogi T 

PROVIDER: S-EPMC2590912 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature