protein

Recombinant Human Aryl hydrocarbon receptor nuclear translocator

MBS968128

0.05 mg (E-Coli)

180 USD

Recombinant Protein

Recombinant Human Aryl hydrocarbon receptor nuclear translocator

Aryl hydrocarbon receptor nuclear translocator

Class E basic helix-loop-helix protein 2; bHLHe2; Dioxin receptor, nuclear translocator; Hypoxia-inducible factor 1-beta; HIF-1-beta; HIF1-beta

aryl hydrocarbon receptor nuclear translocator isoform 4; Aryl hydrocarbon receptor nuclear translocator; aryl hydrocarbon receptor nuclear translocator; aryl hydrocarbon receptor nuclear translocator; Class E basic helix-loop-helix protein 2; bHLHe2; Dioxin receptor, nuclear translocator; Hypoxia-inducible factor 1-beta; HIF-1-beta; HIF1-beta

ARNT

ARNT; ARNT; HIF1B; TANGO; bHLHe2; HIF1BETA; HIF-1beta; HIF1-beta; HIF-1-beta; BHLHE2; ARNT protein; bHLHe2; HIF-1-beta; HIF1-beta

ARNT_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-474

773

MAATTANPEMTSDVPSLGPAIASGNSGPGIQGGGAIVQR
AIKRRPGLDFDDDGEGNSKFLRCDDDQMSNDKERFARSD
DEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVP
TCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKP
SFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTP
VLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTG
RILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGSSS
VDPVSVNRLSFVRNRCRNGLGSVKDGEPHFVVVHCTGYI
KAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNC
TDMSNVCQPTEFISRHNIEGIFTFVDHRCVATVGYQPQE
LLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRF
RSKNQEWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSS
QEPRPT

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

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

Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.

Cloning of a factor required for activity of the Ah (dioxin) receptor.Hoffman E.C., Reyes H., Chu F.-F., Sander F., Conley L.H., Brooks B.A., Hankinson O.Science 252:954-958(1991) Scheel J.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) Homo sapiens protein coding cDNA.Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Towards a catalog of human genes and proteins sequencing and analysis of 500 novel complete protein coding human cDNAs.Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.Genome Res. 11:422-435(2001) NIEHS SNPs programThe 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)

309747071

NP_001184254.1

NM_001197325.1

P27540

54.83kD

AhR Pathway (755436); Angiogenesis Pathway (198772); Cellular Response To Hypoxia Pathway (1270415); Cellular Responses To Stress Pathway (1270414); Chemical Carcinogenesis Pathway (673221); Chemical Carcinogenesis Pathway (673237); HIF-1 Signaling Pathway (695200); HIF-1-alpha Transcription Factor Network Pathway (138045); HIF-2-alpha Transcription Factor Network Pathway (137956); Hypoxic And Oxygen Homeostasis Regulation Of HIF-1-alpha Pathway (138056)

This gene encodes a protein containing a basic helix-loop-helix domain and two characteristic PAS domains along with a PAC domain. The encoded protein binds to ligand-bound aryl hydrocarbon receptor and aids in the movement of this complex to the nucleus, where it promotes the expression of genes involved in xenobiotic metabolism. This protein is also a co-factor for transcriptional regulation by hypoxia-inducible factor 1. Chromosomal translocation of this locus with the ETV6 (ets variant 6) gene on chromosome 12 have been described in leukemias. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2013]

ARNT: a bHLH transcription factor that requires dimerization with another bHLH protein for efficient DNA binding. A binding partner for the Ah (dioxin) nuclear receptor. Required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. A binding partner for HIF1A or HIF2A, transcription factors that regulates transcription from RNA polymerase II promoter in the adaptive response to hypoxia and oxidative stress. This complex activates target genes that limit oxygen consumption. HIF-1alpha may have nontranscriptional activities that inhibit DNA replication and cell proliferation when oxygen becomes scarce. Forms heterodimers with other bHLH proteins. Interacts with TACC3. Three isoforms of the human protein are produced by alternative splicing. Protein type: Nuclear receptor; Transcription factor; DNA-binding; Motility/polarity/chemotaxis. Chromosomal Location of Human Ortholog: 1q21. Cellular Component: cytoplasm; nucleoplasm; nucleus. Molecular Function: aryl hydrocarbon receptor activity; aryl hydrocarbon receptor binding; protein binding; protein heterodimerization activity; RNA polymerase II transcription factor activity, enhancer binding; sequence-specific DNA binding; transcription coactivator activity; transcription factor activity; transcription factor binding. Biological Process: cell differentiation; embryonic placenta development; intracellular receptor-mediated signaling pathway; mRNA transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; positive regulation of erythrocyte differentiation; positive regulation of glycolysis; positive regulation of hormone biosynthetic process; positive regulation of protein sumoylation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; positive regulation of vascular endothelial growth factor receptor signaling pathway; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; response to hypoxia; transcription, DNA-dependent

0.05 mg (E-Coli)

180 USD

0.05 mg (Yeast)

260

0.2 mg (E-Coli)

490

0.2 mg (Yeast)

600

0.5 mg (E-Coli)

715