AHA2 anchors within the cytoplasm membrane of plant cell. In prokaryotic expression system, the protein can’t be recombinant expressed. In Saccharomyces?cerevisiae expression system, the procedures of AHA2 purification stay complex and expensive. By means of RT-PCR and molecular cloning, we constructed an eukaryotic expression vector of AHA2 with PiChia as host. By method of affinity chromatography and gel filtration chromatography, we obtained target protein in highly active with high quality.
