Dihydroorotate dehydrogenase Recombinant Protein | DHODH recombinant protein

Recombinant Human Dihydroorotate dehydrogenase (quinone), mitochondrial

Cat. Num. AAA18438

• Gene Names: DHODH; URA1; POADS; DHOdehase
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Dihydroorotate dehydrogenase; Recombinant Human Dihydroorotate dehydrogenase (quinone); mitochondrial; Dihydroorotate oxidase; DHODH 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: 31-395. Partial
• Sequence: TGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR

• 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 DHODH recombinant protein

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Product Categories/Family for DHODH recombinant protein

Metabolism

References

Cloning and sequencing of a human cDNA coding for dihydroorotate dehydrogenase by complementation of the corresponding yeast mutant.Minet M., Dufour M.E., Lacroute F.Gene 121:393-396(1992) Recombinant human dihydroorotate dehydrogenase expression, purification, and characterization of a catalytically functional truncated enzyme.Copeland R.A., Davis J.P., Dowling R.L., Lombardo D., Murphy K.B., Patterson T.A.Arch. Biochem. Biophys. 323:79-86(1995) 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) Functional expression of a fragment of human dihydroorotate dehydrogenase by means of the baculovirus expression vector system, and kinetic investigation of the purified recombinant enzyme.Knecht W., Bergjohann U., Gonski S., Kirschbaum B., Loeffler M.Eur. J. Biochem. 240:292-301(1996) Requirements for the mitochondrial import and localization of dihydroorotate dehydrogenase.Rawls J., Knecht W., Diekert K., Lill R., Loeffler M.Eur. J. Biochem. 267:2079-2087(2000) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents.Liu S., Neidhardt E.A., Grossman T.H., Ocain T., Clardy J.Structure 8:25-33(2000) Dual binding mode of a novel series of DHODH inhibitors.Baumgartner R., Walloschek M., Kralik M., Gotschlich A., Tasler S., Mies J., Leban J.J. Med. Chem. 49:1239-1247(2006) Exome sequencing identifies the cause of a Mendelian disorder.Ng S.B., Buckingham K.J., Lee C., Bigham A.W., Tabor H.K., Dent K.M., Huff C.D., Shannon P.T., Jabs E.W., Nickerson D.A., Shendure J., Bamshad M.J.Nat. Genet. 42:30-35(2010)

NCBI and Uniprot Product Information

• NCBI GI #: 45006951
• NCBI GeneID: 1723
• NCBI Accession #: NP_001352.2
• NCBI GenBank Nucleotide #: NM_001361.4
• UniProt Accession #: Q02127; Q6P176; A8K8C8
• Molecular Weight: 43.6 kDa
• NCBI Official Full Name: dihydroorotate dehydrogenase (quinone), mitochondrial
• NCBI Official Synonym Full Names: dihydroorotate dehydrogenase (quinone)
• NCBI Official Symbol: DHODH
• NCBI Official Synonym Symbols: URA1; POADS; DHOdehase
• NCBI Protein Information: dihydroorotate dehydrogenase (quinone), mitochondrial
• UniProt Protein Name: Dihydroorotate dehydrogenase (quinone), mitochondrial
• UniProt Gene Name: DHODH
• UniProt Synonym Gene Names: DHOdehase
• UniProt Entry Name: PYRD_HUMAN