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Papers Published

1. Hassouneh, W; Christensen, T; Chilkoti, A, Elastin-like polypeptides as a purification tag for recombinant proteins., Current protocols in protein science, vol. Chapter 6 (August, 2010), pp. 6.11.1-6.11.16 [20814933], [doi] .
   (last updated on 2025/04/17)

   Abstract:
   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.