Recombinant Human Cysteine Dioxygenase CDO1 protein
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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%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO, CDO-I, CDO1
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
Additional notes
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.
General info
Function
Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen.
Sequence similarities
Belongs to the cysteine dioxygenase family.
Post-translational modifications
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.
Target data
Product promise
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