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

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Catalog # MBS967278
Unit / Price
  0.01 mg (E-Coli)  /  $150 +1 FREE 8GB USB
  0.01 mg (Yeast)  /  $170 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $220 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
  0.1 mg (Yeast)  /  $345 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $545 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $900 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $1,050 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
  0.05 mg (Mammalian-Cell)  /  $1,300 +1 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $1,335 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,410 +1 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $1,915 +2 FREE 8GB USB
  0.1 mg (Mammalian-Cell)  /  $1,965 +2 FREE 8GB USB
  1 mg (Baculovirus)  /  $2,525 +3 FREE 8GB USB
SDS-PAGE
Product Name

Indoleamine 2,3-dioxygenase 1 (IDO1), Recombinant Protein

Popular Item
Also Known As

Recombinant Human Indoleamine 2,3-dioxygenase 1

Product Synonym Names
Indoleamine-pyrrole 2,3-dioxygenase
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
1-403. Full length.
Sequence Length
403
Sequence
MAHAMENSWT ISKEYHIDEE VGFALPNPQE NLPDFYNDWM FIAKHLPDLI ESGQLRERVE KLNMLSIDHL TDHKSQRLAR LVLGCITMAY VWGKGHGDVR KVLPRNIAVP YCQLSKKLEL PPILVYADCV LANWKKKDPN KPLTYENMDV LFSFRDGDCS KGFFLVSLLV EIAAASAIKV IPTVFKAMQM QERDTLLKAL LEIASCLEKA LQVFHQIHDH VNPKAFFSVL RIYLSGWKGN PQLSDGLVYE GFWEDPKEFA GGSAGQSSVF QCF DVLLG IQQTAGGGHA AQFLQDMRRY MPPAHRNFLC SLESNPSVRE FVLSKGDAGL REAYDACVKA LVSLRSYHLQ IVTKYILIPA SQQPKENKTS EDPSKLEAKG TGGTDLMNFL KTVRSTTEKS LLKEG
OMIM
147435
3D Structure
ModBase 3D Structure for P14902
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of IDO1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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

IDO1 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for IDO1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
49.4kD
NCBI Official Full Name
indoleamine 2,3-dioxygenase 1
NCBI Official Synonym Full Names
indoleamine 2,3-dioxygenase 1
NCBI Official Symbol
NCBI Official Synonym Symbols
IDO; INDO; IDO-1
  [Similar Products]
NCBI Protein Information
indoleamine 2,3-dioxygenase 1
UniProt Protein Name
Indoleamine 2,3-dioxygenase 1
UniProt Synonym Protein Names
Indoleamine-pyrrole 2,3-dioxygenase
UniProt Gene Name
UniProt Synonym Gene Names
IDO; INDO; IDO-1  [Similar Products]
UniProt Entry Name
I23O1_HUMAN
NCBI Summary for IDO1
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 Comments for IDO1
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
Product References and Citations for IDO1 recombinant protein
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)

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