Tryptophan 2,3-dioxygenase (TDO) is a heme-containing dioxygenase catalyzing the addition of molecular oxygen across the 2,3-double bond of the indole ring of tryptophan to form N-formylkynurenine (NFK). In Anopheles gambiae, TDO is the only enzyme able to catalyze the first and rate-limiting step in L-Trp catabolism through the kynurenine pathway. Tryptophan is an essential amino acid for protein synthesis and also the precursor for production of a number of neurotransmitters, such as serotonin and melatonin; in mosquitoes, the kynurenine pathway is essential for eye pigmentation. Conceivably, the tryptophan-using pathways should be regulated in a coordinated manner in mosquitoes as well as in other species and TDO activation/ inactivation processes could play an essential role in these phenomena.
Recombinant protein corresponding to full-length Anopheles gambiae TDO, fused to His-tag at N-terminal, expressed in E. coli.
Molecular Weight:~47.9kD
Applications:Can be used to test potential kynurenine pathway inhibitors in the mosquito, by continuously monitoring the rate of NFK formation at 321nm (E=3152/Mcm) in in vitro spectrophotometric assays.
Biological Activity:Specific activity towards L-Trp: 87umol/hr/mg. TDO catalyzes the oxidative opening of the L-tryptophan indole moiety to yield N-formylkynurenine (NFK).
Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：50ug
Source Antigen：Recombinant, E. coli
Grade：Highly Purified
Purity：≥98% (SDS-PAGE)
Form：Supplied as a liquid in 50mM sodium phosphate, pH 8.0, 0.15M sodium chloride, 0.2M imidazole,10% glycerol.
