Thermo Scientific Pierce Glutathione Sepharose is a high-performance polymer for the affinity purification of GST-tagged fusion proteins from cell lysates. Capacity, high performance resin.

Characteristics of glutathione agarose:

•Slurry—cross-linked 6% beaded agarose, slurry in sodium azide aqueous solution Status
•High Capacity—can bind at least 40 mg of purified recombinant GST protein/ml of resin
•High Yield and Purity—continues to purify for at least 10 mg GST-tagged protein/ml resin with a purity greater than 90%
•Cost Savings—The resin is affordable and can be reused at least five times without loss of binding capacity and purification performance
• Universal—can effectively purify GST fusion proteins from bacterial lysates or be used with pre-purified GST-tagged proteins to reduce protein interactions
•Good compatibility— Proven effective for use with Thermo Scientific Cell Lysis Reagents for extraction and purification from bacterial and mammalian cell cultures

The high-quality support consists of glutathione, which acts through The 12-atom spacer arms of the central sulfhydryl group are anchored to cross-linked 6% beaded agarose. The use of glutathione (GSH) agarose beads to purify GST fusion proteins is well documented and can be adapted to a variety of scales, column formats, and special applications. Whether the goal is to purify large quantities of recombinant proteins from overexpressing E. coli lysates or to study protein interactions with a GST-tagged bait protein, Pierce Glutathione Sepharose is suitable for the job.

Pierce Glutathione Sepharose efficiently purifies high levels of overexpressed GST-tagged fusion proteins from bacterial lysates such as those obtained using Thermo Scientific B-PER Bacterial Protein Extraction Reagent.

Pierce Glutathione Sepharose performs well in batch binding and spin column procedures at a variety of scales. Performance equals or exceeds that of commonly used GSH resins from other suppliers.

Pierce Glutathione Sepharose is a high quality, stable and elastic affinity support. Various tests confirm that its performance does not degrade after at least five repeated uses. These data demonstrate that the resin is highly resistant to structural degradation or ligand leaching during normal use.

Expression and purification of recombinant proteins are critical for the study of protein regulation, structure and function. Most recombinant proteins are expressed as fusions containing short affinity tags or small proteins such as glutathione S-transferase (GST). This protein can specifically bind to reduced glutathione (GSH) under near-neutral, non-denaturing conditions (such as Tris buffer). Bound proteins can be easily dissociated (eluted) using competitive displacement using buffers containing free, reduced GSH (oxidized glutathione (GSSH) is not suitable for this purpose). When the target protein is expressed as a GST-containing fusion and glutathione is immobilized on a solid support, this protein substrate system enables affinity purification of recombinant proteins and a variety of other experiments related to these proteins.

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