Work

Elastin‐Like Polypeptides as a Purification Tag for Recombinant Proteins

Year: 2010

Type: article

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.

Source: Current Protocols in Protein Science

DOI: 10.1002/0471140864.ps0611s61

Authors: Wafa Hassouneh, Trine Christensen, Ashutosh Chilkoti

Institution: Duke University

Language: English

Topic: Protein purification and stability

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: Elastin Fusion Proteins