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Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2, and GSTM2, is a cytoplasm protein that belongs to the GST superfamily and Mu family. GSTM2 / GST4 contains one GST C-terminal domain and one GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Butyrate, an important luminal component produced from the fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotective by increasing detoxification capabilities in the colon mucosa.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
100 μg | $600 | 7-10 days |
Biological Activity | Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
Description | Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2, and GSTM2, is a cytoplasm protein that belongs to the GST superfamily and Mu family. GSTM2 / GST4 contains one GST C-terminal domain and one GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Butyrate, an important luminal component produced from the fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotective by increasing detoxification capabilities in the colon mucosa. |
Species | Human |
Expression System | E. coli |
Tag | N-His |
Accession Number | P28161 |
Synonyms | GTHMUS,GSTM2-2,GSTM,GST4,glutathione S-transferase mu 2 (muscle) |
Construction | A DNA sequence encoding the native human GSTM2 (P28161) (Met 1-Lys 218) was expressed, with a polyhistide tag at the N-terminus. Predicted N terminal: Met |
Protein Purity | > 97 % as determined by SDS-PAGE |
Molecular Weight | 27.2 kDa (predicted); 27 kDa (reducing conditions) |
Endotoxin | Please contact us for more information. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing 50 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.05% Brig-35, pH 7.5. 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°C. For reconstituted protein solutions, 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 | Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2, and GSTM2, is a cytoplasm protein that belongs to the GST superfamily and Mu family. GSTM2 / GST4 contains one GST C-terminal domain and one GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Butyrate, an important luminal component produced from the fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotective by increasing detoxification capabilities in the colon mucosa. |
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