Adding tags to recombinatnt proteins is a typical means to facilitate the detection of recombinant proteins during expression, and more importantly, to allow simple one-step purification by affinity chromatography resulting in high purity. The Glutathione S-Transferase (GST) is one of the most commonly used tags, which makes the recombinant proteins have a high selective affinity for glutathione. GST-tagged proteins is selectively bound to a glutathione charged medium (GSH), while other cellular proteins bind weakly or are washed out with binding buffers. GST-tagged proteins are eluted under mild, nondenaturing conditions using reduced glutathione. The purification process preserves protein antigenicity and function. If desired, cleavage of the protein from GST can be achieved using a site-specific protease.
We offer products for scaling up purification of GST-tagged proteins with reliable performance.
Glutathione (GSH) Agarose：
Optimized for purification of GST-tagged proteins.
Columns： GSH 1ml；control resin 1ml
Suitable for scaling up purification of GST-tagged proteins, gravity-flow purification, and multiwell plate screening
High binding capacity, up to 100mg/ml medium.
Rapid, one-step performance to high purity>85%, and reproducible.
Compatible with a wide range of reducing agents, detergents, denaturants and other additives.
Sample：E.coli BL21 lysate containing thioredoxin-(his)6
Binding buffer：10mM Na2HPO4，1.8mM KH2PO4，140mM NaCl，2.7mM KCl，pH 7.4
Elution buffer：10mM Glutathione（reduced）, 50mM Tris-HCl, pH 8.0, make as using
1 2 3 4 5 6
3. Wash pool, GSH 1ml；
4.Eluted pool, GSH 1ml；
5.Wash pool,control resin 1ml；
6.Eluted pool, control resin 1ml；
|Highly crossed-linked 6% agarose
|Average paticle size
|Dynamic binding capacity*
|Approx. 10mg GST-tagged protein/ml medium
|Recommended flow rate
|Stable in all commonly used buffers