Name: E.coli Tryptophan Synthase α Chain/Trp A Recombinant Protein
Synonyms: Tryptophan synthase alpha chain;trpA;
Expression host: E.coli
Sequence: Met1-Ser268
Accesstion: P0A877
Species: E.coli
Mol_Mass: 28.7 kDa
AP_Mol_Mass: 27 kDa
Tag: None
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin:
Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Background: Tryptophan synthase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from animals such as humans. Tryptophan synthase typically exists as an α-ββ-α complex.The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.The beta subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Their assembly into a complex leads to structural changes in both subunits resulting in reciprocal activation.
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