Recombinant E.coli Tryptophan Synthase Protein (His Tag) (PKSQ050057)
For research use only.
| Synonyms | Tryptophan synthase, Tryptophan synthetase |
| Species | E.coli |
| Expression Host | E.coli |
| Sequence | Met1-Ser268&Thr2-Ile397 |
| Accession | P0A877&P0A879 |
| Calculated Molecular Weight | 28.7&43.8 kDa |
| Observed Molecular Weight | 28&40-50 kDa |
| Tag | N-His |
| Bio-activity | Not validated for activity |
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles. |
| Shipping | This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C. |
| Formulation | Supplied as a 0.2 μm filtered solution of PBS, pH7.4. |
| Reconstitution | Not Applicable |
| Background | Tryptophan synthase is a multienzyme α2β2 complex composed of two protein subunit. Tryptophan synthase catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The α-subunit catalyzes cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-hydrophobic tunnel to the β-subunit. The β2 subunit contains pyridoxal 5'-phosphate and catalyzes several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target. |
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