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Human Recombinant D-Amino-Acid Oxidase (from E. coli)
Human Recombinant D-Amino-Acid Oxidase (from E. coli)
  75790-648
 :  Prosci
 :  
Human Recombinant D-Amino-Acid Oxidase (from E. coli)
  75790-648
 :  Prosci
 :  92-027
 :  

 

  • Enzyme type:
    Recombinant
  • Source:
    E. coli
  • Species:
    Human
  • Size:
    0.05 mg
  • Tag sequence:
    N-6 His tag
  • Storage Conditions:
    Store at −20 °C, stable for 6 months after receipt. Please minimize freeze−thaw cycles.
  • Endotoxin Content:
    <0.1 ng/ug (1 IEU/ug) as determined by LAL test.
  • Enzyme Name:
    D-Amino-Acid Oxidase
  • Enzyme Synonyms:
    D-Amino-Acid Oxidase, DAAO, DAMOX, DAO
  • Purity:
    >95% as determined by reducing SDS-PAGE
  • Molecular Weight:
    41.64 kD
  • Sequence:
    Met1-Leu347
  • Formulation:
    Supplied as a 0.2 µm filtered solution of 20 mM TrisHCl, 150 mM NaCl, 1 mM DTT, 2 mM EDTA, pH 8.0 . Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
  • Tested Applications:
    Bioassay
  • Cat. No.:
    75790-648
  • Supplier no.:
    92-027

 

 

D-Amino-Acid Oxidase (DAO) belongs to the DAMOX/DASOX family

This recombinant protein can be used for biological assays. For research use only.

Fusion-Tag: N-6 His tag

DAO is a peroxisomal enzyme which founctions as a homodimer to oxidizes D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. D-amino-acid oxidase regulates the level of the neuromodulator D-serine in the brain, has a high activity towards D-DOPA and contributes to dopamine synthesis. D-amino-acid oxidase could act as a detoxifying agent which removes D-amino acids accumulated during aging. It also acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups.