Recombinant Human Cysteine Dioxygenase CDO1 protein is a Human Full Length protein, in the 1 to 200 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
M E Q T E V L K P R T L A D L I R I L H Q L F A G D E V N V E E V Q A I M E A Y E S D P T E W A M Y A K F D Q Y R Y T R N L V D Q G N G K F N L M I L C W G E G H G S S I H D H T N S H C F L K M L Q G N L K E T L F A W P D K K S N E M V K K S E R V L R E N Q C A Y I N D S I G L H R V E N I S H T E P A V S L H L Y S P P F D T C H A F D Q R T G H K N K V T M T F H S K F G I R T P N A T S G S L E N N
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen.
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO, CDO-I, CDO1
Recombinant Human Cysteine Dioxygenase CDO1 protein is a Human Full Length protein, in the 1 to 200 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl
ab153778 is greater than 95% pure, as determined by SEC-HPLC and reducing SDS-PAGE. It is lyophilized from an 0.2 µM filtered solution.
Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen.
Belongs to the cysteine dioxygenase family.
The thioether cross-link between Cys-93 and Tyr-157 plays a structural role through stabilizing the Fe(2+) ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen.
Previously labelled as Cysteine Dioxygenase Type 1.
Cysteine Dioxygenase CDO1 also known as CDO is a non-heme iron enzyme that catalyzes the conversion of L-cysteine to cysteine sulfinic acid. This enzyme plays an important mechanical role in maintaining proper levels of cysteine within cells. With a molecular weight of approximately 23 kDa CDO1 is expressed mainly in the liver although it can be found in various tissues where it helps regulate cysteine concentration and detoxification processes.
Cysteine dioxygenase participates in sulfur metabolism and it functions as a monomer. The enzyme ensures sulfur balance by transforming excess cysteine which can be toxic if accumulated. This metabolic process impacts taurine and sulfate production vitally affecting cellular and systemic functions. CDO1 modulates cellular responses to cysteine levels by contributing to these metabolic pathways providing necessary components for other cellular activities and detoxifying mechanisms.
The oxidation of cysteine by CDO1 feeds into the taurine and hypotaurine metabolism as well as the hydrogen sulfide biosynthesis pathways. These pathways are integral to maintaining cellular redox balance and ion regulation. The enzyme’s activity connects it to proteins like cysteine aminotransferase and sulfite oxidase which further metabolize products from its catalytic activity integrating CDO1 into a broader metabolic network.
Cysteine dioxygenase has associations with neurodegenerative diseases and cancers. Imbalances in CDO1 activity can lead to altered cysteine homeostasis contributing to conditions such as Alzheimer's disease where oxidative stress often plays a role. Additionally dysregulation of CDO1 may influence cancer progression as altered cysteine metabolism is linked to tumor growth and survival. Proteins such as glutamate cysteine ligase may connect to CDO1 through shared pathways affecting oxidative stress and sulfur amino acid metabolism providing insights into disease mechanisms and potential therapeutic targets.
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