Biotechnology Bulletin ›› 2012, Vol. 0 ›› Issue (12): 40-45.

• Review • Previous Articles     Next Articles

Application of Elastin-like Polypeptide Tag for RecombinantProteins Purification

Lin Heng1,2, Xu Chongbo2, Sun Lihui2, Hu Xuejun2   

  1. 1 College of Life Science and Technology,Dalian University,Dalian 116622 ;2 College of Medicine,Dalian University,Dalian 116622
  • Received:2012-05-14 Revised:2013-01-25 Online:2012-12-26 Published:2013-02-06

Abstract: Elastin-like polypeptide(ELP)is an extremely promising recombinant protein purification tag. The artificial polypeptidesconsist of repeats of the pentapeptide(VPGXG)with a reversible phase transition at a specific temperature. ELP fusion protein retains thisbehavior when a target protein is fused to the ELP at the gene level. Once isolating a recombinant ELP fusion protein from the protein solution byrepeating inverse transition cycling(ITC), the ELP tag can be proteolytically removed, or self-cleave mediated by intein in response to solutioncondition shift, then we can recover the pure target protein. At present, the method is used successfully in expression systems such as E.coli andplants. The highest yield of GFP-ELP fusion protein is 1.6 g/L in E.coli. This non-chromatographic purification method is simple, rapid, costeffective,and easy to scale up. This review summarizes mechanism, technical route and development direction of this method.