Indoleamine 2,3-dioxygenase 1 Recombinant Protein | IDO1 recombinant protein

Recombinant Human Indoleamine 2,3-dioxygenase 1

Cat. Num. AAA967278

• Gene Names: IDO1; IDO; INDO; IDO-1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Indoleamine 2; 3-dioxygenase 1; Recombinant Human Indoleamine 2; Indoleamine-pyrrole 2; 3-dioxygenase; IDO1 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: 1-403aa; Full Length
• Sequence: MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
• Sequence Length: 403

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• 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 IDO1 recombinant protein

Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.

Product Categories/Family for IDO1 recombinant protein

Cardiovascular

References

Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA.Dai W., Gupta S.L.Biochem. Biophys. Res. Commun. 168:1-8(1990) Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA.Tone S., Takikawa O., Habara-Ohkubo A., Kadoya A., Yoshida R., Kido R.Nucleic Acids Res. 18:367-367(1990) Gene structure of human indoleamine 2,3-dioxygenase.Kadoya A., Tone S., Maeda H., Minatogawa Y., Kido R.Biochem. Biophys. Res. Commun. 189:530-536(1992) Human indoleamine 2,3-dioxygenase from peripheral blood.He X., Xu L., Liu Y., Zeng Y. 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) Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan.Metz R., Duhadaway J.B., Kamasani U., Laury-Kleintop L., Muller A.J., Prendergast G.C.Cancer Res. 67:7082-7087(2007) Evolution of vertebrate indoleamine 2,3-dioxygenases.Yuasa H.J., Takubo M., Takahashi A., Hasegawa T., Noma H., Suzuki T.J. Mol. Evol. 65:705-714(2007) Crystal structure of human indoleamine 2,3-dioxygenase catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.Sugimoto H., Oda S., Otsuki T., Hino T., Yoshida T., Shiro Y.Proc. Natl. Acad. Sci. U.S.A. 103:2611-2616(2006)

NCBI and Uniprot Product Information

• NCBI GI #: 4504577
• NCBI GeneID: 3620
• NCBI Accession #: NP_002155.1
• NCBI GenBank Nucleotide #: NM_002164.5
• UniProt Accession #: P14902; Q540B4; E5RGR8; F6M9T7
• Molecular Weight: 47.3 kDa
• NCBI Official Full Name: indoleamine 2,3-dioxygenase 1
• NCBI Official Synonym Full Names: indoleamine 2,3-dioxygenase 1
• NCBI Official Symbol: IDO1
• NCBI Official Synonym Symbols: IDO; INDO; IDO-1
• NCBI Protein Information: indoleamine 2,3-dioxygenase 1
• UniProt Protein Name: Indoleamine 2,3-dioxygenase 1
• Protein Family: Indoleamine 2,3-dioxygenase
• UniProt Gene Name: IDO1
• UniProt Synonym Gene Names: IDO; INDO; IDO-1
• UniProt Entry Name: I23O1_HUMAN

NCBI Description

This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.[provided by RefSeq, Feb 2011]

Uniprot Description

INDO: Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen. Belongs to the indoleamine 2,3-dioxygenase family.

Protein type: Cell cycle regulation; Oxidoreductase; EC 1.13.11.52; Amino Acid Metabolism - tryptophan

Chromosomal Location of Human Ortholog: 8p12-p11

Cellular Component: cytosol; smooth muscle contractile fiber; stereocilium bundle

Molecular Function: electron carrier activity; heme binding; indoleamine 2,3-dioxygenase activity; metal ion binding; tryptophan 2,3-dioxygenase activity

Biological Process: cytokine production during acute inflammatory response; female pregnancy; immune system process; multicellular organismal response to stress; negative regulation of interleukin-10 production; negative regulation of T cell proliferation; positive regulation of chronic inflammatory response; positive regulation of interleukin-12 production; positive regulation of T cell tolerance induction; positive regulation of T-helper 2 type immune response; regulation of activated T cell proliferation; response to lipopolysaccharide; tryptophan catabolic process; tryptophan catabolic process to kynurenine