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Trp A Protein, E. coli, Recombinant

Catalog No. TMPJ-00819
Synonyms: Tryptophan synthase α chain, trpA, Tryptophan synthase alpha chain

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.

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Trp A Protein, E. coli, Recombinant
Pack Size Availability Price/USD Quantity
10 μg 5 days $ 129.00
50 μg 5 days $ 390.00
500 μg 5 days $ 1,900.00
1 mg 5 days $ 2,730.00
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Biological Description
Technical Params
Product Properties
Description 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.
Species E.coli
Expression System E. coli
Tag None
Accession Number P0A877
Synonyms Tryptophan synthase α chain, trpA, Tryptophan synthase alpha chain
Amino Acid Met1-Ser268
Construction Recombinant E.coli Tryptophan Synthase Alpha Chain is produced by our E.coli expression system and the target gene encoding Met1-Ser268 is expressed.
Protein Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight 27 KDa, reducing conditions
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.
Stability & Storage

Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.

Shipping

The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.

Research 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.

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Keywords

Trp A Protein, E. coli, Recombinant Tryptophan synthase α chain trpA Tryptophan synthase alpha chain Tryptophan synthase a chain recombinant recombinant-proteins proteins protein

 

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