Reduced glutathione is covalently linked to High Resolution Agarose 6B-CL for use in affinity purification of glutathione-S-transferase (GST) and GST-fused proteins. This product provides a one step purification method and permits rapid, mild and highly selective purifications of proteins containing glutathione binding sequences. Glutathione-Agarose is prepared by covalently coupling glutathione to epoxy-activated highly crosslinked 6% agarose beads to form a stable thioether linkage. The coupling was optimized to give a high binding capacity of 5 mg or more of Glutathione-S-transferase (GST) per ml of wet gel. Bound GST –fusion proteins are easily displaced from the resin by elution with buffers containing reduced glutathione. Mild elution conditions preserve protein antigenicity and function.Glutathione HR ensures the lowest sample dilution and best high-resolution separation.
• Ligand: Reduced glutathione (GSH)
• Matrix: Agarose 6B-CL (highly crosslinked agarose beads, 6%)
• Average Particle size: 38 µm
• Molecular weight range: 6 x 104 – 2 x 107
• Matrix activation: Epoxy
• Matrix spacer: 12 atoms
• Ligand density: 5 – 10 mg GST / ml drained gel
• Binding capacity: 8 mg recombinant GST-tagged protein / ml drained gel
• pH stability: 3 – 12
Research or further manufacturing use only, not for food or drug use.