Product Description

Recombinant E. coli Trp synthase (N-6His)

Size: 50µg

Catalogue Number: EPT234-50

Lead times: 1-2 weeks, if manufacturer has product in stock

Manufacturer/Ship Location: China

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-Å 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.

Description: 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.

Alternate Names: Tryptophan synthetase, Tryptophan synthase

Purity: Greater than 95% as determined by reducing SDS-PAGE.

Endotoxin: Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.

Molecular Weight: 28.7&43.8 KDa

Observed Molecular Weight: 28&40-50 KDa, reducing conditions

Storage: Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.

Storage Conditions: Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Delivery Condition: The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.

Accession: P0A877&P0A879

Research Use Only