Description
Recombinant E.coli Tryptophan Synthase Protein (His Tag) | PKSQ050057 | Gentaur US, UK & Europe Disrtribition
Synonyms: Tryptophan synthetase; Tryptophan synthase
Active Protein: N/A
Activity: Recombinant E.coli Tryptophan synthase is produced by our E.coli expression system and the target gene encoding Met1-Ser268&Thr2-Ile397 is expressed with a 6His tag at the N-terminus.
Protein Construction: Recombinant E.coli Tryptophan synthase is produced by our E.coli expression system and the target gene encoding Met1-Ser268&Thr2-Ile397 is expressed with a 6His tag at the N-terminus.
Fusion Tag: N-His
Species: E.coli
Expressed Host: E.coli
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.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 72.5 kDa
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.
Research Area: N/A
