TDO2 Human

Tryptophan 2,3-Dioxygenase Human Recombinant
Cat. No.
BT20916
Source
Escherichia Coli.
Synonyms
Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

TDO2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 426 amino acids (1-406 a.a.) and having a molecular mass of 50kDa. The TDO2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
TDO2, a ferrous heme enzyme, catalyzes the initial and rate-limiting step in the kynurenine pathway, the primary metabolic route for tryptophan. This enzyme incorporates oxygen into the indole ring of tryptophan. TDO2 exhibits broad substrate specificity, acting on tryptamine and its derivatives, including D- and L-tryptophan, 5-hydroxytryptophan, and serotonin.
Description
Recombinant human TDO2, expressed in E. coli, is a monomeric, non-glycosylated polypeptide chain. This protein, with a molecular weight of 50 kDa, consists of 426 amino acids (residues 1-406) and includes an N-terminal 20 amino acid His-tag. Purification of TDO2 is achieved using proprietary chromatographic methods.
Physical Appearance
A sterile, colorless solution, free of particulates.
Formulation
The TDO2 solution is supplied at a concentration of 0.25 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.2 M NaCl, 5 mM DTT, 1 mM EDTA, and 30% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity is determined to be greater than 90.0% using SDS-PAGE analysis.
Synonyms
Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD.

Product Science Overview

Introduction

Tryptophan 2,3-dioxygenase (TDO2) is a heme-containing enzyme that plays a crucial role in the metabolism of the essential amino acid tryptophan. This enzyme catalyzes the first and rate-limiting step in the kynurenine pathway, which is the oxidative cleavage of the indole ring of tryptophan to form N-formylkynurenine .

Gene and Protein Structure

The TDO2 gene is located on chromosome 4q32.1 in humans . The gene encodes a protein that forms a homo-tetrameric structure, with each monomer having a molecular weight of approximately 48 kDa . The active enzyme complex is around 190 kDa in size . The enzyme contains a heme prosthetic group, which is essential for its catalytic activity .

Function and Mechanism

TDO2 is primarily expressed in the liver, but it is also found in other tissues such as the brain and placenta . The enzyme’s primary function is to regulate systemic tryptophan levels by catalyzing its degradation along the kynurenine pathway . This pathway is significant for the production of several bioactive metabolites, including kynurenine, which can be further metabolized into nicotinamide adenine dinucleotide (NAD+), an essential coenzyme in cellular metabolism .

The reaction catalyzed by TDO2 involves the incorporation of molecular oxygen into tryptophan, resulting in the formation of N-formylkynurenine. This reaction is the first and rate-limiting step in the kynurenine pathway .

Clinical Significance

TDO2 has been implicated in various physiological and pathological processes. Increased activity of TDO2 and subsequent production of kynurenine have been associated with immune suppression in cancer . This is because kynurenine and its metabolites can modulate immune responses, potentially aiding tumor cells in evading immune surveillance .

Additionally, single nucleotide polymorphisms (SNPs) in the TDO2 gene have been linked to disorders such as autism and hypertryptophanemia . The enzyme’s role in tryptophan metabolism also makes it a potential target for therapeutic interventions in diseases where tryptophan catabolism is dysregulated .

Recombinant TDO2

Recombinant human TDO2 is produced using genetic engineering techniques, where the TDO2 gene is cloned and expressed in suitable host cells. This allows for the production of large quantities of the enzyme for research and therapeutic purposes . Recombinant TDO2 retains the same structural and functional properties as the native enzyme, making it a valuable tool for studying tryptophan metabolism and developing potential therapeutic agents .

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