Recombinant E.coli Tryptophan Synthase α Chain/Trp A Protein

SKU: PKSQ050056

Size: 50μg

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 < -20℃ for 3 months.

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Exp date: 12 months

Category ID_II: Recombinant Proteins

Category ID_III: Others

Abbreviation: Tryptophan Synthase α Chain;Trp A

Target Synonym: Tryptophan synthase alpha chain;trpA

Research Areas:

Conjugation:

Target Species: E.coli

Expression Host: E.coli

Application:

Fusion tag: None

UNIProt ID: P0A877

Accession: P0A877

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.

Concentration:

Activity: Not validated for activity

Sequence: Met1-Ser268

Purity: > 95 % as determined by reducing SDS-PAGE.

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 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.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Calculated MW: 28.7 kDa

ObservedMW: 27 kDa