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Purification of GST-tagged Proteins

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).

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 comparably large GST-tag might sometimes interfere with these downstream applications. In these cases it is easily removed by protease cleavage e.g. by Factor Xa provided that a specific protease sequence is located between the protein domain and GST.

Glutathione Magnetic Agarose Beads

Ferrimagnetic agarose beads suitable for fast & efficient small-scale purification of GST and GST tagged proteins.

Glutathione Agarose

High-performance 4 % agarose suitable for FPLC, gravity flow and batch purification of GST and GST tagged proteins.