Kynurenine 3-monooxygenase Recombinant Protein | KMO recombinant protein

Recombinant Human Kynurenine 3-monooxygenase

Cat. Num. AAA1119330

• Gene Names: KMO; dJ317G22.1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Kynurenine 3-monooxygenase; Recombinant Human Kynurenine 3-monooxygenase; Kynurenine 3-hydroxylase; KMO 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: 1-486aa; Full Length
• Sequence: MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKKPRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCVLLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLSMYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKKVINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQISNLISR

• 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 KMO recombinant protein

Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract.

Product Categories/Family for KMO recombinant protein

Metabolism

References

Cloning and functional expression of human kynurenine 3-monooxygenase.Alberati-Giani D., Cesura A.M., Broger C., Warren W.D., Rover S., Malherbe P.FEBS Lett. 410:407-412(1997) Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase.Breton J., Avanzi N., Magagnin S., Covini N., Magistrelli G., Cozzi L., Isacchi A.Eur. J. Biochem. 267:1092-1099(2000) Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase.Breton J., Avanzi N., Magagnin S., Covini N., Magistrelli G., Cozzi L., Isacchi A.Eur. J. Biochem. 267:1092-1099(2000) . The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Endogenous kynurenines as targets for drug discovery and development.Stone T.W., Darlington L.G.Nat. Rev. Drug Discov. 1:609-620(2002)

NCBI and Uniprot Product Information

• NCBI GI #: 187960045
• NCBI GeneID: 8564
• NCBI Accession #: NP_003670.2
• NCBI GenBank Nucleotide #: NM_003679.4
• UniProt Accession #: O15229; Q5SY07; Q5SY08; Q5SY09; A2A2U8; A2A2U9; A2A2V0
• Molecular Weight: 57.8 kDa
• NCBI Official Full Name: kynurenine 3-monooxygenase
• NCBI Official Synonym Full Names: kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)
• NCBI Official Symbol: KMO
• NCBI Official Synonym Symbols: dJ317G22.1
• NCBI Protein Information: kynurenine 3-monooxygenase
• UniProt Protein Name: Kynurenine 3-monooxygenase
• Protein Family: Kynurenine 3-monooxygenase
• UniProt Gene Name: KMO
• UniProt Entry Name: KMO_HUMAN

NCBI Description

This gene encodes a mitochondrion outer membrane protein that catalyzes the hydroxylation of L-tryptophan metabolite, L-kynurenine, to form L-3-hydroxykynurenine. Studies in yeast identified this gene as a therapeutic target for Huntington disease. [provided by RefSeq, Oct 2011]

Uniprot Description

KMO: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract. Belongs to the aromatic-ring hydroxylase family. KMO subfamily. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Mitochondrial; Amino Acid Metabolism - tryptophan; Oxidoreductase; EC 1.14.13.9; Membrane protein, multi-pass; Membrane protein, integral

Chromosomal Location of Human Ortholog: 1q42-q44

Cellular Component: cytosol; integral to membrane; mitochondrial inner membrane; mitochondrial outer membrane

Molecular Function: FAD binding; kynurenine 3-monooxygenase activity; NAD(P)H oxidase activity

Biological Process: anthranilate metabolic process; NAD metabolic process; quinolinate biosynthetic process; response to salt stress; tryptophan catabolic process; tryptophan catabolic process to kynurenine