Bacteria-Derived Salmonella Tryptophan synthase Recombinant Protein N-6 His Tag Lyophilized from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in Lyophilized from a 0.2 um filtered solution of PBS, pH7.4. It is not recommended to reconstitute to a concentration less than 100UG/ml. Dissolve the lyophilized protein in ddH2O. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Bacteria-Derived Target: IL36G Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: E. coli 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.
Additional Information:
Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-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 beta -subunit. The beta 2 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. This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.
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