D-Amino-Acid Oxidase (DAO) (Center) Peptide

Details for Product No. ABIN691860, Supplier: Log in to see
Protein Name
  • daao
  • oxda
  • damox
  • dao
  • DAO
  • DKFZp469N2232
  • zgc:77858
  • zgc:76928
  • SC5F2A.23c
  • wu:fb55b11
  • zgc:113922
  • MGC114783
  • Abp
  • Abp1
  • 1600012D06Rik
  • DAAO
  • AI987963
  • Dao-1
  • Dao1
  • OXDA
  • D-amino-acid oxidase
  • LOC100037820
  • D-amino-acid oxidase, tandem duplicate 3
  • D-amino-acid oxidase, tandem duplicate 2
  • D-amino acid oxidase
  • D-amino-acid oxidase, tandem duplicate 1
  • amine oxidase, copper containing 1
  • amine oxidase, copper-containing 1
  • dao
  • pco075778
  • DAO
  • oxda
  • dao.3
  • dao.2
  • SCO6740
  • dao.1
  • PTRG_02224
  • SJAG_02496
  • Aoc1
  • DAO1
  • Dao
Protein Region
Peptide Type
Blocking Peptide (BP)
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Specificity The synthetic peptide sequence used to generate the antibody AP13941c was selected from the Center region of DAO. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Background This gene encodes the peroxisomal enzyme D-amino acid oxidase. The enzyme is a flavoprotein which uses flavin adenine dinucleotide (FAD) as its prosthetic group. Its substrates include a wide variety of D-amino acids, but it is inactive on the naturally occurring L-amino acids. Its biological function is not known, it may act as a detoxifying agent which removes D-amino acids that accumulate during aging. In mice, it degrades D-serine, a co-agonist of the NMDA receptor. This gene may play a role in the pathophysiology of schizophrenia.
Restrictions For Research Use only
Storage 4
Storage Comment Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Expiry Date 6 months
Background publications Mitchell, Paul, Chen, Morris, Payling, Falchi, Habgood, Panoutsou, Winkler, Tisato, Hajitou, Smith, Vance, Shaw, Mazarakis, de Belleroche: "Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 107, Issue 16, pp. 7556-61, 2010 (PubMed).