Tryptophan synthase beta chain Recombinant Protein

• 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 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 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.

• NCBI Gene ID:

  945768

• Swiss Prot:

  P0A879

• Accession Number:

  P0A879

• Tag:

  N-6 His tag

• Type:

  Recombinant Proteins

• Source:

  E. coli

• Buffer:

  Lyophilized from a 0.2 um filtered solution of PBS, pH7.4. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the lyophilized protein in ddH2O.

• Shipping Conditions:

  Room Temp

• Calculated Molecular Weight:

  43.8 kD

• Applications Notes:

  This recombinant protein can be used for biological assays. For research use only.

• NCBI Official Name:

  Tryptophan synthase, beta subunit

• NCBI Organism:

  Escherichia coli str. K-12 substr. MG1655

• Other Product Names:

  Tryptophan synthase beta chain, trpB, Trp B

• Species:

  E. coli

• Physical Properties:

  Lyophilized

• CAS Number:

  9000-83-3