protein

Recombinant Human D-amino-acid oxidase

MBS948863

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human D-amino-acid oxidase

D-amino-acid oxidase

D-amino-acid oxidase; D-amino-acid oxidase; D-amino-acid oxidase; D-amino-acid oxidase

DAO

DAO; DAO; DAAO; OXDA; DAMOX; DAMOX; DAAO; DAMOX; DAO

OXDA_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-347; Full length

347

MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRF
TPLTTTDVAAGLWQPYLSDPNNPQEADWSQQTFDYLLSH
VHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKL
TPRELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERG
VKFFQRKVESFEEVAREGADVIVNCTGVWAGALQRDPLL
QPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQ
TVTLGGIFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNA
RIIGERTGFRPVRPQIRLEREQLRTGPSNTEVIHNYGHG
GYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Metabolism

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 roves 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.

Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase.Momoi K., Fukui K., Watanabe F., Miyake Y.FEBS Lett. 238:180-184(1988) Momoi K.Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004)

148539837

NP_001908.3

NM_001917.4

P14920

55.45kD

Arginine And Proline Metabolism Pathway (82957); Arginine And Proline Metabolism Pathway (323); D-Arginine And D-ornithine Metabolism Pathway (82972); D-Arginine And D-ornithine Metabolism Pathway (341); Glycine, Serine And Threonine Metabolism Pathway (82949); Glycine, Serine And Threonine Metabolism Pathway (313); Glyoxylate Metabolism And Glycine Degradation Pathway (1270180); Metabolic Pathways (132956); Metabolism Pathway (1269956); Metabolism Of Amino Acids And Derivatives Pathway (1270158)

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. [provided by RefSeq, Jul 2008]

DAO: 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. Belongs to the DAMOX/DASOX family. Protein type: Oxidoreductase; EC 1.4.3.3; Amino Acid Metabolism - glycine, serine and threonine; Amino Acid Metabolism - arginine and proline; Other Amino Acids Metabolism - D-Arginine and D-ornithine. Chromosomal Location of Human Ortholog: 12q24. Cellular Component: cytosol; mitochondrial outer membrane; peroxisomal matrix; peroxisomal membrane; peroxisome. Molecular Function: cofactor binding; D-amino-acid oxidase activity; protein binding; protein dimerization activity; receptor binding. Biological Process: dopamine biosynthetic process; glyoxylate metabolic process; proline catabolic process. Disease: Schizophrenia

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750