D-Amino-Acid Oxidase (DAO) (Center) Peptide
| Name | D-Amino-Acid Oxidase (DAO) |
| Synonyms |
Dao, daao, oxda, damox, dao, DAO, Dao1, DAAO, OXDA, DAMOX, MGC35381, DKFZp469N2232, Dao-1, AI987963, MGC77858, zgc:77858, MGC76928, zgc:76928, SC5F2A.23c, DAO1, MGC113922, wu:fb55b11, zgc:113922, MGC1 ...
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| Binding Site |
Center |
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1 reference available |
| Certificates | ISO 9001:2008 |
| Catalog no. | ABIN691860 |
| Quantity | 0.1 mg |
| Price | 49.50 $ Plus shipping costs $45.00 |
| Shipping to |
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| Availability | Will be delivered in 2 to 3 Business Days |
Additional Information
| Immunogen | Synthetic peptide |
| Characteristics | Blocking peptide for DAO (Center) antibody ABIN657862 |
| 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. |
| Comments |
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. |
| Synonyms | Dao, daao, oxda, damox, dao, DAO, Dao1, DAAO, OXDA, DAMOX, MGC35381, DKFZp469N2232, Dao-1, AI987963, MGC77858, zgc:77858, MGC76928, zgc:76928, SC5F2A.23c, DAO1, MGC113922, wu:fb55b11, zgc:113922, MGC114783 |
Application Details
| Storage | 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 |
| Restrictions | For Research Use only |
Publications
| Product |
Mitchell, Paul, Chen et al.: "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).
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