UNIT 6.11 Elastin-Like Polypeptides as a Purification Tag for Recombinant Proteins

  1. Wafa Hassouneh,
  2. Trine Christensen,
  3. Ashutosh Chilkoti

Published Online: 1 AUG 2010

DOI: 10.1002/0471140864.ps0611s61

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Hassouneh, W., Christensen, T. and Chilkoti, A. 2010. Elastin-Like Polypeptides as a Purification Tag for Recombinant Proteins. Current Protocols in Protein Science. 61:6.11:6.11.1–6.11.16.

Author Information

  1. Duke University, Durham, North Carolina

Publication History

  1. Published Online: 1 AUG 2010
  2. Published Print: AUG 2010


This unit presents a recombinant protein purification method that employs an elastin-like polypeptide (ELP) as a purification tag. ELPs undergo a sharp and reversible phase transition when heated above their lower critical solution temperature. ELPs retain this behavior when they are fused to a protein, and thereby provide a simple method to isolate a recombinant ELP fusion protein from cell contaminants by cycling the solution through the insoluble and soluble phase of the ELP fusion protein using a procedure that is termed Inverse Transition Cycling. This method does not require the use of chromatography, so it is cost-effective, easy to scale up, and easy to multiplex. Curr. Protoc. Protein Sci. 61:6.11.1-6.11.16. © 2010 by John Wiley & Sons, Inc.


  • Elastin-like polypeptides (ELP);
  • inverse transition cycling (ITC);
  • purification tag;
  • recombinant protein;
  • non-chromatographic purification;
  • protein fusion;
  • transition temperature