DDT Human
D-Dopachrome Tautomerase Human Recombinant
Cat. No.
BT5561
Source
Escherichia Coli.
Synonyms
EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.
Appearance
Sterile filtered colorless 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.
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Description
DDT Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 14.8 kDa. The DDT is fused to a 20 amino acids His-Tag at N-terminus and 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). As a member of the lyase family, specifically the carboxy-lyases, DDT facilitates the cleavage of carbon-carbon bonds. Notably, DDT exhibits a 33% amino acid sequence homology with macrophage migration inhibitory factor (MIF) and possesses comparable tautomerase activity. Functionally, DDT acts as a proinflammatory cytokine.
Description
Recombinant human DDT, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 138 amino acids (residues 1-118) and exhibiting a molecular weight of 14.8 kDa. The DDT protein is fused to a 20 amino acid His-Tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The DDT human solution is supplied in a buffer containing 20mM Tris-HCl at a pH of 8 and 10% glycerol.
Stability
For optimal storage, the product should be kept at 4°C if the entire vial is expected to be used within 2-4 weeks. For extended storage, it is recommended to store the product frozen at -20°C. To further enhance long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is advisable. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of the product is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL.
Product Science Overview
Introduction
Structure and Function
D-DT is structurally and functionally related to MIF, sharing significant sequence homology and enzyme activity. It catalyzes the conversion of D-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA), a key intermediate in melanin biosynthesis . The gene encoding D-DT is located on chromosome 22, closely linked to the MIF gene .
Biological Roles
D-DT has been implicated in various biological processes, including:
- Inflammation: Like MIF, D-DT acts as a pro-inflammatory cytokine, playing a role in the immune response and inflammation .
- Cardiovascular Diseases: Emerging evidence suggests that D-DT may have a role in cardiovascular diseases, although its exact mechanisms are still under investigation .
- Cancer: D-DT has been studied in the context of neoplastic processes, indicating its potential involvement in cancer progression .
Recombinant D-DT
Recombinant D-DT is produced using recombinant DNA technology, which involves inserting the D-DT gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its structure, function, and potential therapeutic uses .
Research and Therapeutic Potential
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