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ELK Biotechnology
SKU:EPT234
Recombinant E.coli Trp synthase (N-6His)
Recombinant E.coli Trp synthase (N-6His)
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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.
Accession: P0A877&P0A879
Molecular weight: 28.7&43.8 KDa
Apparent molecular weight: 28&40-50 KDa, reducing conditions
Other names: Tryptophan synthetase; Tryptophan synthase
Storage condition: 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.
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.
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.
Delivery condition: The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
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.
Accession: P0A877&P0A879
Molecular weight: 28.7&43.8 KDa
Apparent molecular weight: 28&40-50 KDa, reducing conditions
Other names: Tryptophan synthetase; Tryptophan synthase
Storage condition: 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.
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.
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.
Delivery condition: The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
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.
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