Glutathione S-transferase (GST) is a 26 kDa protein derived from Schistosoma japonicum. GST enzymes from various sources, both native and recombinantly expressed as fusion to the N-terminus of target proteins, are easily purified in a one-step procedure by affinity chromatography on immobilized glutathione (Glutathione Agarose, Fast Flow).
Due to the positive influence of the GST-tag on protein solubility and expression efficiency especially of small proteins, this technique has been widely used to generate proteins for crystallization, molecular immunology studies and studies involving protein-protein and protein-DNA interactions.
However, the GST-tag might sometimes interfere with these downstream applications. In these cases it is easily removed by protease cleavage e.g. by Factor Xa (GST Cleavage Capture Kit) provided that a specific protease sequence is located between the protein domain and GST.
Furthermore, free GST or GST fusion proteins are conveniently detected by Western blotting using GST antibody.

