Specifications
- Pk:50 µG
- Enzyme type:Recombinant
- Source:E. coli
- Species:E. coli
- Tag sequence:N-6 His tag
- 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.
- Enzyme name:Tryptophan synthase beta chain
- Purity:>95% as determined by reducing SDS-PAGE
- Molecular weight:43.8 kDa
- 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.
Specifications
About this item
Tryptophan synthase is an enzyme that catalyses 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 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 catalyse 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.
Fusion-Tag: N-6 His tag
This recombinant protein can be used for biological assays. For research use only.