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Specifications
- Enzyme type:Recombinant
- Source:E. coli
- Species:E. coli
- Size:0.05 mg
- 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.
- Endotoxin content:<0.1 ng/ug (1 IEU/ug) as determined by LAL test.
- Enzyme name:Tryptophan synthase beta chain
- Enzyme synonyms:Tryptophan synthase beta chain, trpB, Trp B
- Purity:>95% as determined by reducing SDS-PAGE
- Molecular weight:43.8 kD
- Sequence:Thr2-Ile397
- Formulation:Lyophilized from a 0.2 µm filtered solution of PBS,pH 7.4. Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the Lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
- Cat. no.:75791-808
- Supplier No.:92-623
Specifications
About this item
Tryptophan synthase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan
This recombinant protein can be used for biological assays. For research use only.
Fusion-Tag: N-6 His tag
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 alpha- beta beta - alpha 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.