Description
Recombinant E.coli Tryptophan Synthase β Chain/Trp B Protein (His Tag) | PKSQ050055 | Gentaur US, UK & Europe Disrtribition
Synonyms: Tryptophan synthase beta chain; trpB
Active Protein: N/A
Activity: Recombinant E.coli Tryptophan synthase beta chain is produced by our E.coli expression system and the target gene encoding Thr2-Ile397 is expressed with a 6His tag at the N-terminus.
Protein Construction: Recombinant E.coli Tryptophan synthase beta chain is produced by our E.coli expression system and the target gene encoding Thr2-Ile397 is expressed with a 6His tag at the N-terminus.
Fusion Tag: N-His
Species: E.coli
Expressed Host: E.coli
Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 43.8 kDa
Formulation: Supplied as a 0.2 μm filtered solution of PBS, pH7.4.
Reconstitution: Not Applicable
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.
Research Area: N/A
