These Glutathione spin columns provide a fast, easy-to-use format to purify GST-fusion proteins from cellular lysates.

• Binds at least 40 mg of purified recombinant GST protein per mL of resin
• Consistently purifies at least 10 mg of GST-tagged protein per mLl of resin with greater than 90% purity
• Resin can be reused at least five times without reduction in binding capacity and purification performance
• Works well to purify GST-fusion proteins from bacterial lysates or use with pre-purified GST-tagged proteins to pull down protein interactions
• Validated and effective for use with Cell Lysis Reagents to extract and purify from bacterial or mammalian cell cultures

Pierce Glutathione Agarose effectively purifies high levels of overexpressed GST-tagged fusion proteins from bacterial lysates, such as those that are obtained with B-PER Bacterial Protein Extraction Reagents.

Pierce Glutathione Agarose performs well in batch-binding and spin-column procedures at a variety of scales. Performance equals or exceeds popular GSH resins.

The expression and purification of recombinant proteins is central to protein regulation, structure and function studies. The majority of recombinant proteins are expressed as fusions with short affinity tags or small proteins, such as glutathione S-transferase (GST). This protein binds specifically to reduced glutathione (GSH) in near-neutral, nondenaturing conditions (e.g., Tris buffer). Bound protein is easily dissociated (eluted) by competitive displacement with buffer containing free, reduced GSH (oxidized glutathione, GSSH is not effective for this purpose). When proteins of interest are expressed as fusions with GST and glutathione is immobilized to an solid support, this protein-substrate system enables affinity purification of recombinant proteins, as well as various other experiments with those proteins.