CDO1 Human

Cysteine Dioxygenase Human Recombinant
Cat. No.
BT19874
Source
Escherichia Coli.
Synonyms
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.
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

CDO1 Human Recombinant fused with a 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-170 a.a.) and having a molecular mass of 23.9kDa.
The CDO1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Cysteine dioxygenase (CDO1), a non-heme iron enzyme found in mammals, plays a crucial role in initiating various metabolic pathways. These pathways involve pyruvate and sulfur-containing compounds such as sulfate, hypotaurine, and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid by incorporating dioxygen. This enzyme is essential for regulating cellular cysteine levels, particularly in the liver, where it maintains intracellular free cysteine concentrations within a narrow range. CDO1 influences both intracellular cysteine and glutathione levels. High expression levels of CDO1 are observed in the liver and placenta, while lower levels are found in the heart, brain, and pancreas. CDO1 expression has also been detected in HepG2 hepatoblastoma cells.
Description
Recombinant human CDO1, fused with a 37 amino acid His tag at the N-terminus, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain containing 207 amino acids (residues 1-170), resulting in a molecular weight of 23.9 kDa. Purification of CDO1 is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The CDO1 solution is supplied in 20mM Tris buffer (pH 8.0), with 10% glycerol and 1mM DTT.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90.0% by SDS-PAGE analysis.
Synonyms
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR.

Product Science Overview

Structure and Function

CDO is a 22.5 kDa protein that contains 200 amino acid residues and has an isoelectric point (pI) of 5.5 . The primary structure of CDO is highly conserved among mammalian species, with only minor differences between murine and human CDO . The enzyme is part of the cupin superfamily, characterized by a 6-stranded β-barrel in a “jelly-roll” topology . Crystal structures of the protein have been obtained at high resolution, providing detailed insights into its active site and overall structure .

The active site of CDO contains iron (II) bound to the cysteine substrate and key residues that facilitate the catalytic process . The enzyme oxidizes cysteine to cysteine sulfinic acid by incorporating dioxygen (O₂), although the exact mechanism of this reaction is still under investigation .

Biological Role

CDO is highly expressed in the liver and placenta, with lower expression levels in the heart, brain, and pancreas . It is also detectable in hepatoblastoma HepG2 cells . The enzyme is a vital regulator of cellular cysteine concentrations and plays an essential role in maintaining the hepatic concentration of intracellular free cysteine within a narrow range .

By converting cysteine to cysteine sulfinic acid, CDO helps regulate intracellular levels of cysteine and responds to changes in cysteine availability . This regulation is crucial for preventing cysteine toxicity and ensuring proper cellular function . CDO is also involved in the biosynthesis of taurine, a compound important for various physiological processes .

Recombinant Human CDO

Recombinant human CDO is produced using expression systems such as Escherichia coli (E. coli) . The recombinant protein is typically purified to high levels of purity and is used for research purposes to study the enzyme’s structure, function, and role in various biological processes .

The recombinant human CDO protein is supplied as a filtered solution and is stable for several months when stored at temperatures below -20°C . It is used in various biochemical assays and studies to understand the enzyme’s catalytic mechanisms and its implications in health and disease .

Clinical and Research Implications

CDO has been implicated in various neurodegenerative diseases and cancers, likely related to cysteine toxicity . Understanding the enzyme’s function and regulation can provide insights into these conditions and potentially lead to therapeutic interventions .

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