Specifications
- Pk:50 µG
- Enzyme type:Recombinant
- Source:E. coli
- Species:Salmonella typhimurium (strain LT2/SGSC1412/ATCC 700720)
- 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
- Purity:>95% as determined by reducing SDS-PAGE
- Molecular weight:72,3 kDa
- Sequence:Met1-Ala268&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 a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses 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 beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses 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.
Fusion-Tag: N-6 His tag
This recombinant protein can be used for biological assays. For research use only.