Abstract:

Objective: To establish a new cost-effective method for purification of the recombinant protein; Method: Recombinant proteins expressed in E. coli were separated by using SDS-PAGE. Target proteins were isolated by cutting the gel slices that contain the right bands which were stained by 0.25 mol/L KCl instead of 4 mol/L NaAc solution. We selected the modified experimental procedures of including repeated freezing and thawing then high-speed centrifugation to replace that of the original overnight dialysis after dialysis bag-electrophoresis elution. Results: We improved the experimental efficiency significantly. Proteins purified by this modified method remained proper antigenicity when detected by ELISA and Western blot. Discussion: Compared with other conventional ways of protein purification, this method is relatively simple and effective, especially suitable for the general laboratorys.