Publication Abstract from PubMed
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.
Novel affinity tag system using structurally defined antibody-tag interaction: application to single-step protein purification.,Nogi T, Sangawa T, Tabata S, Nagae M, Tamura-Kawakami K, Beppu A, Hattori M, Yasui N, Takagi J Protein Sci. 2008 Dec;17(12):2120-6. Epub 2008 Sep 11. PMID:18787202[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
