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Mouse Anti-DAO Recombinant Antibody (B-3) (CBMAB-D0195-YC)

Provided herein is a Mouse monoclonal antibody, which binds to D-Amino Acid Oxidase (DAO). The antibody can be used for immunoassay techniques, such as WB, IP, IF, ELISA.
See all DAO antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
B-3
Antibody Isotype
IgG
Application
WB, IP, IF, ELISA

Basic Information

Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
D-Amino Acid Oxidase
Introduction
DAO is 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.
Entrez Gene ID
Human1610
Mouse13142
Rat114027
UniProt ID
HumanP14920
MouseP18894
RatO35078
Alternative Names
D-Amino Acid Oxidase; EC 1.4.3.3; DAMOX; DAAO; D-Amino-Acid Oxidase; EC 1.4.3; OXDA;
Function
Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. 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. Does not act on acidic amino acids.
Biological Process
Carboxylic acid metabolic process Source: Reactome
D-alanine catabolic process Source: UniProtKB
D-amino acid catabolic process Source: GO_Central
Dopamine biosynthetic process Source: UniProtKB
D-serine catabolic process Source: UniProtKB
D-serine metabolic process Source: UniProtKB
Proline catabolic process Source: UniProtKB
Protein localization Source: Reactome
Cellular Location
Peroxisome
Involvement in disease
Schizophrenia (SCZD):
A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder.

Padhi, A. K., & Hazra, S. (2019). Insights into the role of d‐amino acid oxidase mutations in amyotrophic lateral sclerosis. Journal of cellular biochemistry, 120(2), 2180-2197.

Nagano, T., Yamao, S., Terachi, A., Yarimizu, H., Itoh, H., Katasho, R., ... & Kamada, S. (2019). D-amino acid oxidase promotes cellular senescence via the production of reactive oxygen species. Life science alliance, 2(1).

Chen, Y. C., Chou, W. H., Tsou, H. H., Fang, C. P., Liu, T. H., Tsao, H. H., ... & Liu, Y. L. (2019). A post-hoc study of D-amino acid oxidase in blood as an Indicator of post-stroke dementia. Frontiers in neurology, 10, 402.

Sasabe, J., & Suzuki, M. (2018). Emerging role of d-amino acid metabolism in the innate defense. Frontiers in microbiology, 9, 933.

Kondori, N. R., Paul, P., Robbins, J. P., Liu, K., Hildyard, J. C., Wells, D. J., & De Belleroche, J. S. (2018). Focus on the role of D-serine and D-amino acid oxidase in amyotrophic lateral sclerosis/motor neuron disease (ALS). Frontiers in molecular biosciences, 5, 8.

Du, S., Wang, Y., Weatherly, C. A., Holden, K., & Armstrong, D. W. (2018). Variations of L-and D-amino acid levels in the brain of wild-type and mutant mice lacking D-amino acid oxidase activity. Analytical and bioanalytical chemistry, 410(12), 2971-2979.

Lin, H., Hu, H., Duan, W., Liu, Y., Tan, G., Li, Z., ... & Li, C. (2018). Intramuscular delivery of scAAV9-hIGF1 prolongs survival in the hSOD1G93A ALS mouse model via upregulation of D-amino acid oxidase. Molecular Neurobiology, 55(1), 682-695.

Jagannath, V., Marinova, Z., Monoranu, C. M., Walitza, S., & Grünblatt, E. (2017). Expression of D-amino acid oxidase (DAO/DAAO) and D-amino acid oxidase activator (DAOA/G72) during development and aging in the human post-mortem brain. Frontiers in neuroanatomy, 11, 31.

Lin, C. H., Yang, H. T., Chiu, C. C., & Lane, H. Y. (2017). Blood levels of D-amino acid oxidase vs. D-amino acids in reflecting cognitive aging. Scientific reports, 7(1), 1-10.

Koga, R., Miyoshi, Y., Sakaue, H., Hamase, K., & Konno, R. (2017). Mouse d-amino-acid oxidase: distribution and physiological substrates. Frontiers in molecular biosciences, 4, 82.

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For research use only. Not intended for any clinical use.

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