DDT Mouse

D-Dopachrome Tautomerase Mouse Recombinant
Cat. No.
BT5646
Source
Escherichia Coli.
Synonyms

D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

Appearance
Sterile Filtered clear solution.
Purity

Greater than 95.0% 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

DDT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-118 a.a) and having a molecular mass of 15.5kDa. DDT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Dopachrome tautomerase (DDT) is an enzyme that catalyzes the conversion of D-dopachrome to 5,6-dihydroxyindole (DHI). This enzyme belongs to the carboxy-lyase family, specifically those that cleave carbon-carbon bonds. DDT shares a 33% sequence homology with macrophage migration inhibitory factor (MIF) and exhibits similar tautomerase activity. Functionally, DDT acts as a pro-inflammatory cytokine.
Description
Recombinant DDT from Mouse has been expressed in E. coli. This non-glycosylated polypeptide consists of 141 amino acids (residues 1-118), resulting in a molecular weight of 15.5 kDa. A 23-amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved through proprietary chromatographic methods.
Physical Appearance
Clear solution, sterile filtered.
Formulation
The DDT protein solution is supplied at a concentration of 1 mg/ml and contains 20 mM Tris-Hcl buffer (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advised. Repeated freeze-thaw cycles should be avoided.
Purity
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
Synonyms

D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMPFVELE TNLPASRIPA GLENRLCAAT ATILDKPEDR VSVTIRPGMT LLMNKSTEPC AHLLVSSIGV VGTAEQNRTH SASFFKFLTE ELSLDQDRIV IRFFPLEAWQ IGKKGTVMTF L

Product Science Overview

Introduction

D-Dopachrome Tautomerase (D-DT), also known as D-dopachrome decarboxylase, is an enzyme that plays a significant role in various biological processes. It is a protein-coding gene found in mice and is homologous to the human DDT gene. This enzyme is involved in the tautomerization of D-dopachrome to 5,6-dihydroxyindole (DHI), a key step in the melanin biosynthesis pathway.

Gene and Protein Structure

The Ddt gene is located on chromosome 10 in mice, specifically at the position 75607067-75609208 bp on the negative strand . The gene encodes a protein that shares structural and functional similarities with the macrophage migration inhibitory factor (MIF), another important cytokine involved in immune responses .

Biological Function

D-DT is known to bind to the CD74 receptor with high affinity, leading to the activation of ERK1/2 MAP kinase and downstream proinflammatory pathways . This binding and subsequent activation play a crucial role in the immune response, particularly in the regulation of inflammation. The enzyme is also highly expressed in murine cardiomyocytes and is secreted by the heart after ischemic stress, indicating its protective role in cardiac function .

Recombinant Production

Recombinant D-DT is produced using various expression systems, including bacterial, yeast, and mammalian cells. The recombinant protein is often used in research to study its function and potential therapeutic applications. The production process involves cloning the Ddt gene into an expression vector, transforming the host cells, and purifying the expressed protein.

Clinical and Research Implications

Research has shown that D-DT levels correlate with disease severity in conditions such as sepsis and malignancy . The enzyme’s role in immune regulation and its protective effects in cardiac function make it a potential target for therapeutic interventions. Additionally, the study of recombinant D-DT helps in understanding its physiological and pathological roles, providing insights into the development of new treatments for inflammatory and cardiovascular diseases.

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