Rapid high-yield expression and purification of fully post-translationally modified recombinant clusterin and mutants.

ABSTRACT: The first described and best known mammalian secreted chaperone, abundant in human blood, is clusterin. Recent independent studies are now exploring the potential use of clusterin as a therapeutic in a variety of disease contexts. In the past, the extensive post-translational processing of clusterin, coupled with its potent binding to essentially any misfolded protein, have meant that its expression as a fully functional recombinant protein has been very difficult. We report here the first rapid and high-yield system for the expression and purification of fully post-translationally modified and chaperone-active clusterin. Only 5-6 days is required from initial transfection to harvest of the protein-free culture medium containing the recombinant product. Purification to near-homogeneity can

SUBMITTER: Satapathy S 

PROVIDER: S-EPMC7455699 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature