Tryptophan synthase Recombinant Protein Cat. No.: 92-668

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psi-iconSpecifications
SPECIES:Salmonella typhimurium (strain LT2/SGSC1412/ATCC 700720)
SOURCE SPECIES:E. coli
SEQUENCE:Met1-Ala268&Thr2-Ile397
FUSION TAG:N-6 His tag
TESTED APPLICATIONS:
APPLICATIONS:This recombinant protein can be used for biological assays. For research use only.
psi-iconProperties
PURITY:Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test.
PREDICTED MOLECULAR WEIGHT:72.3 kD
PHYSICAL STATE:Lyophilized
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.
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.
psi-iconAdditional Info
ALTERNATE NAMES:Tryptophan synthetase, Tryptophan synthase
ACCESSION NO.:Q9NZH8
OFFICIAL SYMBOL:IL36G
GENE ID:56300
psi-iconBackground and References
BACKGROUND:Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyzes the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyzes 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 catalyzes 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.

FOR RESEARCH USE ONLY.

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