Aldehyde oxidase Recombinant Protein | AOX1 recombinant protein

Recombinant Human Aldehyde oxidase

Cat. Num. AAA1265127

• Gene Names: AOX1; AO; AOH1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Aldehyde oxidase; Recombinant Human Aldehyde oxidase; Aldehyde oxidase 1; Azaheterocycle hydroxylase (EC:1.17.3.-); AOX1 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 236-421. Partial, provide FAD-binding PCMH-type Domain
• Sequence: FGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRK

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for AOX1 recombinant protein

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N-methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis

Product Categories/Family for AOX1 recombinant protein

Metabolism

References

cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase.Wright R.M., Vaitaitis G.M., Wilson C.M., Repine T.B., Terada L.S., Repine J.E.Proc. Natl. Acad. Sci. U.S.A. 90:10690-10694(1993) Molecular cloning, refined chromosomal mapping, and structural analysis of the human gene encoding aldehyde oxidase (AOX1) , a candidate for the ALS2 gene.Wright R.M., Weigel L.K., Varella-Garcia M., Vaitaitis G., Repine J.E.Redox Rep. 3:135-144(1997) Mutation of human molybdenum cofactor sulfurase gene is responsible to classical xanthinuria type II.Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T.Biochem. Biophys. Res. Commun. 282:1194-1200(2001) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005)

NCBI and Uniprot Product Information

• NCBI GI #: 71773480
• NCBI GeneID: 316
• NCBI Accession #: NP_001150.3
• NCBI GenBank Nucleotide #: NM_001159.3
• UniProt Accession #: Q06278; O14765; Q53RR8; Q53TV3; Q9BYF0; Q9UPG6
• Molecular Weight: 24.6 kDa
• NCBI Official Full Name: aldehyde oxidase
• NCBI Official Synonym Full Names: aldehyde oxidase 1
• NCBI Official Symbol: AOX1
• NCBI Official Synonym Symbols: AO; AOH1
• NCBI Protein Information: aldehyde oxidase
• UniProt Protein Name: Aldehyde oxidase
• Protein Family: Alcohol oxidase
• UniProt Gene Name: AOX1
• UniProt Synonym Gene Names: AO
• UniProt Entry Name: AOXA_HUMAN

NCBI Description

Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide. Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis. [provided by RefSeq, Jul 2008]

Uniprot Description

AOX1: Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide. Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis. [provided by RefSeq, Jul 2008]

Protein type: EC 1.2.3.1; Oxidoreductase; Amino Acid Metabolism - tryptophan; Cofactor and Vitamin Metabolism - vitamin B6; Amino Acid Metabolism - tyrosine; Xenobiotic Metabolism - drug metabolism - cytochrome P450; Cofactor and Vitamin Metabolism - nicotinate and nicotinamide; Amino Acid Metabolism - valine, leucine and isoleucine degradation

Chromosomal Location of Human Ortholog: 2q33

Cellular Component: cytoplasm; cytosol

Molecular Function: 2 iron, 2 sulfur cluster binding; aldehyde oxidase activity; electron carrier activity; FAD binding; iron ion binding; molybdopterin cofactor binding; NAD binding; oxidoreductase activity, acting on CH-OH group of donors; xanthine dehydrogenase activity

Biological Process: inflammatory response; vitamin B6 metabolic process; vitamin metabolic process; water-soluble vitamin metabolic process; xanthine catabolic process