Application
Tagged proteins can be purified directly from pretreated bacterial lysates using GSTrap 4B. 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 whose recognition sequence is located immediately upstream from the multiple cloning site on the pGEX plasmids. GST-tagged proteins can be detected using colorimetric or immunological methods. The medium, Glutathione Sepharose 4B, is also available as lab packages and is a good choice for scale-up. The columns can be operated with a syringe, peristaltic pump, or liquid chromatography system such as AKTA design or FPLC System.
Features and Benefits
High binding capacity. Mild elution conditions preserving protein antigenicity and function. Easy one-step purifications of Glutathione S-Transferase (GST) tagged proteins resulting in high purity. GSTrap 4B are designed to be used with a syringe, pump, or chromatography system, such as AKTA design.
General description
GSTrap 4B columns are prepacked Glutathione Sepharose 4B columns for convenient, high capacity one-step purification of glutathione S-transferase (GST) tagged proteins.
Legal Information
GSTrap is a trademark of Cytiva
Storage and Stability
Store at 4 to 30 °C (20% Ethanol)
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