Cysteine dioxygenase (CDO1) is a mammalian non-heme iron enzyme that initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. This protein catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is critical regulator of cellular cysteine concentrations and has an important role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. Recombinant CDO1 protein , expressed in E. coli and purified by using conventional chromatography techniques. Source: Recombinant corresponding to human Cysteine dioxygenase, aa1-170, his-tagged, expressed in E. coli. AA Sequence: MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR. Enzyme Activity: Not determined. This product is recommended for use in applications that do not require a catalytically active form of the protein. Storage and Stability: Aliquot to avoid repeated freezing and thawing and freeze at -70C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 6 months.
