Affinity purification of glutathione-S-transferase (GST) and GST fusion proteins frequently utilizes covalently linked glutathione. Glutathione Agarose Resin contains glutathione covalently bound to agarose beads for use in affinity purification of glutathione-S-transferase (GST) and GST fusion proteins as it has a high binding affinity and specificity to the Glutathione S-transferase (GST) protein. GST-tagged proteins can be highly purified and bound GST-tagged proteins are easily eluted from the resin with buffers containing reduced glutathione.
Fusion proteins expressed from pGEX vectors contain a Glutathione S-transferase (GST) moiety and can therefore be purified to near homogeneity by affinity chromatography on glutathione as a substrate in inactivate toxic small molecules via formation of mercapturic acid. Since the affinity of GST for its substrate lies in the submillimolar range, immobilization of glutathione on an agarose matrix makes a highly efficient affinity chromatography resin.
Our product offers a rapid and convenient one-step purification method for proteins containing glutathione binding sequences with high selectivity where bound GST–fusion proteins are easily dissociated from the resin by using elution buffers containing reduced glutathione.
- One-step process; high-capacity affinity purification of recombinant GST-tagged proteins
- Compatible with both small and large protein complexes
- Basic procedure, no need for optimization
- Suitable for batch and column purification
5 ml, 10 ml, 25 ml