CDO1 (cysteine dioxygenase, type I) belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis (1). CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine (1,2). CDO1 exists as a monomer and is expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart (1). CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell (3,4).1) McCann KP, Akbari MT, Williams AC, et al. Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA. Biochim. Biophys. Acta 1994; 1209:107-10.
Immunogen
CDO1 antibody was raised against a 19 amino acid peptide near the amino terminus of human CDO1. The immunogen is located within amino acids 30 - 80 of CDO1.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WB
CDO1 antibody can be used for detection of CDO1 by Western blot at 1 - 2 μg/ml.