A versatile ionic strength sensitive tag from a human GM-CSF-derived linear epitope
Related Experiment Video
Updated: May 10, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Norma Perotti1, Marina Etcheverrigaray, Ricardo Kratje
1Cell Culture Laboratory, School of Biochemistry and Biological Sciences, Universidad Nacional del Litoral, Santa Fe, Argentina.
Abstract:
A 7-mer hGM-CSF-derived linear epitope (APARSPS) is herein described as a novel and small tag taking into account its particular binding affinity in native conditions that could be easily modified by increasing or lowering the ionic strength. Thus, a 3.4 or 3.8-fold binding increment was observed in high NaCl concentration when the tag was fused to IFN-α2b or when the peptide was in its native environment, respectively. The high salt concentration increased the affinity of the binding interaction and improved the APARSPS epitope binding to the paratope allowing one to design an immunoaffinity chromatography purification step in which the high ionic strength was useful to adsorb the fusion protein to the immunoaffinity matrix and the low ionic strength at pH 9 was valuable to desorb it (a 470-fold purification with a 94%-purity was attained in only one step). Also, this short tag did not affect the functionality of the fusion protein and it was able to be detected both in the natural molecule (hGM-CSF) as in the tagged one with the same high detection limit: 273pg of each protein.

