GST-Tag Purification

Introduction of GST-Tag Purification

Glutathione S-transferase(GST) has a relative molecular mass of about 26,000 Da, a macromolecular protein derived from Schistosoma japonicum. GST can specifically combine with glutathione, acting as an enzyme and a substrate. Using this principle, GST is made into a tag to express a fusion protein, which specifically binds to an affinity medium with a glutathione ligand, thereby purifying the target protein, and then using a specific enzyme to remove the GST tag to obtain a natural protein.

Fig 1. Schematic presentation of Glutathione Affinity chromatography. (Schäfer F, et al., 2015)

In protein research, if you want to obtain highly soluble proteins, you can give priority to the GST fusion expression system.

The Superiority of His-Tag Purification

• Increase the solubility of exogenous protein
• Well-preserved protein antigenicity and biological activity
• Expressed in different hosts with a wide range of applications
• Rapid removal with different proteases
• Improve the stability of exogenous protein
• High specificity
• Easy and gentle purification

Advantages of Our Products

• One-step rapid purification of GST-tagged proteins
• Excellent magnification
• Higher resolution
• Fully maintain the original function and activity of the protein
• Highly specific binding
• GST-Tag is widely used in biological experiments to ensure the purity and quality of protein samples and promote protein solubility.

Applications of Our Products

• Purify soluble protein
• Detection of the target protein
• Pull-down experiments to study protein-protein interactions

Creative BioMart can provide you with various specifications of GST-Tag purification-related products for the purification and separation of target proteins in the fields of proteomics, drug screening, and cell biology research. You can quickly find the reagents you need by searching keywords such as CAT number or product name. Please tell us your product needs, we will provide you with a comprehensive consultation. If you have any questions, please feel free to contact us.

Reference:

1. Schäfer F, Seip N, Maertens B, et al. (2015) Purification of GST-Tagged Proteins. Methods in Enzymology. 559: 127-139.