Thermo Scientific Pierce Glutathione Agarose is a high-capacity, high-performance resin for affinity purification of GST-tagged fusion proteins from cellular lysates.

Features of Glutathione Agarose:

• Slurry—crosslinked 6% beaded agarose, slurried in water with sodium azide
• High capacity—binds at least 40 mg of purified recombinant GST protein per milliliter of resin
• High yield and purity—consistently purifies at least 10 mg of GST-tagged protein per milliliter of resin with greater than 90% purity
• Cost-effective—resin is economically priced and can be reused at least five times without reduction in binding capacity and purification performance
• Versatile—works well to purify GST-fusion proteins from bacterial lysates or use with pre-purified GST-tagged proteins to pull down protein interactions
• Compatible—validated and effective for use with Thermo Scientific Cell Lysis Reagents to extract and purify from bacterial or mammalian cell cultures

The high-quality support consists of glutathione that has been immobilized by its central sulfhydryl group via a 12-atom spacer arm to crosslinked 6% beaded agarose. Purification of GST-fusion proteins using glutathione (GSH) agarose beads is well documented and adaptable to a variety of scales, column formats and specific applications. Whether the purpose is to purify large amounts of recombinant protein from over-expressing E. coli lysates or to investigate protein interactions involving GST-tagged bait proteins, Pierce Glutathione Agarose is suitable for the task.

Pierce Glutathione Agarose effectively purifies high levels of overexpressed GST-tagged fusion proteins from bacterial lysates, such as those that are obtained with Thermo Scientific 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 from other suppliers.

Pierce Glutathione Agarose is a high-quality, stable and resilient affinity support. Tests confirm that no decrease in performance occurs after at least five repeated uses. These data indicated that the resin is highly resistant to structural degradation or ligand leaching during normal use.

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.

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