Recombinant OXDD protein (His tag)

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Recombinant Human D-aspartate oxidase (DDO) fragment (amino acids 1-341) is a high-purity, stable protein product designed for structural and biochemical studies. This fragment retains key functional domains and offers excellent solubility, making it ideal for investigating the enzyme's role in regulating acidic D-amino acid metabolism and neuroprotection.

D-aspartate oxidase (DDO) is a human enzyme that selectively catalyzes the oxidative deamination of acidic D-amino acids, particularly D-aspartate. By suppressing D-aspartate levels in the brain, DDO protects against excitotoxicity as D-aspartate can act as an agonist for glutamate receptors. The enzyme also plays a protective role against D-amino acid toxicity throughout the body, with additional functions suggested in intestinal metabolism. DDO is primarily localized to the peroxisomal matrix, where it performs its catalytic activity, though it has also been detected in the cytosol. This recombinant fragment encompasses the complete functional domain (residues 1-341) and maintains the enzyme's structural integrity for research applications.

1-341