Production and purification of recombinant GST-fusion proteins of Ang-1 isoforms.

Recombinant proteins were purified from bacterial lysates by glutathione Sepharose 4B chromatography and analyzed by SDS-PAGE followed by Coomassie blue staining. The expected molecular weights of fusion proteins were obtained and purified to near homogeneity by this procedure. Lanes 1, 2, 3, and 4 (0.7-, 9.9-, 1.3-, and 1.5-kb isoforms, respectively).