| Host: | HEK293 cells |
| Note: | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Formulation: | Lyophilised from a 0.22 Mu m filtered solution of PBS, pH 7.4. |
| Storage Instruction: | Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
| Determination Method: | Please contact us for more information. |
| Immunogen Region: | Met1-Lys218 |
| Immunogen: | Recombinant Schistosoma japonicum GST-His Protein is produced by E. coli expression system. The target protein is expressed with sequence (Met1-Lys218) of schistosoma japonicum GST-His fused with 6×His tag at the C-terminus. |
| Immunogen Sequence: | SPVPPACDPRLLNKLLRDSY LLHSRLSQCPDVNPLSIPVL LPAVDFSLGEWKTQTEQSKA QDILGAVSLLLEGVMAARGQ LEPSCLSSLLGQLSGQVRLL LGALQGLLGTQLPPQGRTTA HKDPSALFLSLQQLLRGKVR FLLLVEGPALCVRRTLPTTA VPSRTSQLLTLNKFPNRTSG LLETNFSVVARTAGPGLLNR LQGFRAKIIPGQLNQTSGSL DQIPGYLNGTHEPVNGTHG |
| 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. |
Information sourced from Uniprot.org