Tryptophan synthase is a multienzyme ?2β2 complex composed of two protein subunit. Tryptophan synthase catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The ?-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.
Product Name:
E.coli Tryptophan Synthase Recombinant Protein (RPES3431)
Product Code:
RPES3431
Size:
10µg
Species:
E.coli
Expressed Host:
E.coli
Synonyms:
Tryptophan synthetase, Tryptophan synthase
Accession:
P0A877&P0A879
Sequence:
Met1-Ser268&Thr2-Ile397
Fusion tag:
N-His
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
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.
Purity:
> 95% as determined by reducing SDS-PAGE.
Mol Mass:
72.5 kDa
AP Mol Mass:
28&40-50 kDa
Formulation:
Supplied as a 0.2 µm filtered solution of PBS, pH7.4.
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.
Stability and Storage:
Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
