Recombinant Human Indoleamine 2,3-dioxygenase 1 | MyBioSource MBS967278 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human Indoleamine 2,3-dioxygenase 1

catalog :

MBS967278

quantity :

0.05 mg (E-Coli)

price :

190 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS967278

products type :

Recombinant Protein

products full name :

Recombinant Human Indoleamine 2,3-dioxygenase 1

products short name :

Indoleamine 2,3-dioxygenase 1

products name syn :

Indoleamine-pyrrole 2,3-dioxygenase

other names :

indoleamine 2,3-dioxygenase 1; Indoleamine 2,3-dioxygenase 1; indoleamine 2,3-dioxygenase 1; indoleamine 2,3-dioxygenase 1; Indoleamine-pyrrole 2,3-dioxygenase

products gene name :

IDO1

other gene names :

IDO1; IDO1; IDO; INDO; IDO-1; IDO; INDO; IDO-1

uniprot entry name :

I23O1_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

1-403

sequence length :

403

sequence :

MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDW
MFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRL
ARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKK
LELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRD
GDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDT
LLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYL
SGWKGNPQLSDGLVYEGFWED

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products categories :

Cardiovascular

products description :

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

products 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 gi num :

4504577

ncbi acc num :

NP_002155.1

ncbi gb acc num :

NM_002164.5

uniprot acc num :

P14902

ncbi mol weight :

49.4kD

ncbi pathways :

African Trypanosomiasis Pathway (194384); African Trypanosomiasis Pathway (194323); Histidine, Lysine, Phenylalanine, Tyrosine, Proline And Tryptophan Catabolism Pathway (1309221); L-kynurenine Degradation Pathway (907939); L-tryptophan Degradation III (eukaryotic) Pathway (139214); L-tryptophan Degradation XI (mammalian, Via Kynurenine) Pathway (139210); L-tryptophan Degradation To 2-amino-3-carboxymuconate Semialdehyde Pathway (139207); Metabolic Pathways (132956); Metabolism Pathway (1269956); Metabolism Of Amino Acids And Derivatives Pathway (1270158)

ncbi summary :

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 summary :

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

size1 :

0.05 mg (E-Coli)

price1 :

190 USD

size2 :

0.05 mg (Yeast)

price2 :

190

size3 :

0.2 mg (E-Coli)

price3 :

460

size4 :

0.2 mg (Yeast)

price4 :

460

size5 :

0.5 mg (Yeast)

price5 :

750

more info or order :

MyBioSource product webpage