Recombinant Human Tryptophan 2,3-Dioxygenase, T7-tagged

• Cat.No.: TDO2-823H
• Product Overview: Recombinant TDO2 protein was expressed in E.coli with T7-tag at the N-terminus. The molecular weight is 47872 Da.

Specification

• Species: Human
• Source: E.coli
• Tag: T7
• Description: In Anopheles gambiae tryptophan 2,3-dioxygenase (TDO) is the only enzyme able to catalyze the first and ratelimiting step in L-Trp catabolism through the kynurenine pathway. On the contrary, in mammals, L-Trp can enter the kynurenine pathway through the alternative action of two enzymes, TDO and Indoleamine 2,3-dioxygenase (IDO). TDO converts L-tryptophan to N- formyl kynurenine by catalyzing the heme-dependent oxidative opening of the substrate indole ring. The metabolism of L-tryptophan (L-Trp) exceeding the protein synthesis requirements proceeds through several routes, generating a number of compounds that play multiple roles in controlling basic aspects of the biology of most living organisms.
• Sequences of amino acids: 1-406 aa
• Formulation: 10 mM Tris. pH 8.0. 0.1% Triton X-100. 0.002% NaN3. 10mM DTT.
• Purity: 95%

Gene Information

• Gene Name: TDO2 tryptophan 2,3-dioxygenase [ Homo sapiens ]
• Synonyms: TDO; TPH2; TRPO; TDO2; tryptophan 2,3-dioxygenase; TO; tryptophanase; tryptophan oxygenase; tryptophan pyrrolase; tryptamin 2,3-dioxygenase;EC 1.13.11.11
• Gene ID: 6999
• mRNA Refseq: NM_005651
• Protein Refseq: NP_005642
• MIM: 191070
• UniProt ID: P48775
• Chromosome Location: 4q31-q32
• Pathway: Metabolic pathways; Tryptophan metabolism; Metabolism of amino acids and derivatives
• Function: amino acid binding; heme binding; metal ion binding; oxidoreductase activity; oxygen binding; oxygen binding; tryptophan 2,3-dioxygenase activity