Genetic engineers have used glutathione S-transferase to create the GST gene fusion system. This system is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's promoter results in expression of a fusion protein: the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. GST is commonly used to create fusion proteins. The tag has the size of 22amino acids(roughly 26 KDa), which, compared to other tags like the Myc- or the FLAG-tag, is quite big. However, many commercially-available sources of GST-tagged plasmids include athrombindomain for cleavage of the GST tag during protein purification.
生物学的情報 | Testing in progress |
説明 | Genetic engineers have used glutathione S-transferase to create the GST gene fusion system. This system is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's promoter results in expression of a fusion protein: the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. GST is commonly used to create fusion proteins. The tag has the size of 22amino acids(roughly 26 KDa), which, compared to other tags like the Myc- or the FLAG-tag, is quite big. However, many commercially-available sources of GST-tagged plasmids include athrombindomain for cleavage of the GST tag during protein purification. |
Species | Schistosoma japonicum |
Expression Host | Baculovirus Insect Cells |
Tag | Tag Free |
Accession Number | P08515 |
Construction | The Glutathione S-transferase (P08515) (Met 1-Lys 218), with additional 11 amino acids at the C-terminus, was expressed and purified. |
Protein Purity | > 95 % as determined by SDS-PAGE |
分子量 | 26.9 kDa (predicted) |
Endotoxin | < 1.0 EU/μg of the protein as determined by the LAL method. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing 50 mM Tris, 100 mM NaCl, 2 mM GSH, pH 8.0.Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization. |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage |
It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping |
In general, Lyophilized powders are shipping with blue ice. |
Research Background | Genetic engineers have used glutathione S-transferase to create the GST gene fusion system. This system is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's promoter results in expression of a fusion protein: the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. GST is commonly used to create fusion proteins. The tag has the size of 22amino acids(roughly 26 KDa), which, compared to other tags like the Myc- or the FLAG-tag, is quite big. However, many commercially-available sources of GST-tagged plasmids include athrombindomain for cleavage of the GST tag during protein purification. |
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