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Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150) (170 kDa glucose-regulated protein) (GRP-170)

 HYOU1_HUMAN             Reviewed;         999 AA.
Q9Y4L1; A8C1Z0; B7Z909; Q2I204; Q53H25;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 178.
RecName: Full=Hypoxia up-regulated protein 1;
AltName: Full=150 kDa oxygen-regulated protein;
Short=ORP-150;
AltName: Full=170 kDa glucose-regulated protein;
Short=GRP-170;
Flags: Precursor;
Name=HYOU1; Synonyms=GRP170, ORP150;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Astrocytoma;
PubMed=9020069; DOI=10.1006/bbrc.1996.5890;
Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T.,
Matsumoto M., Yura T., Yanagi H.;
"Cloning and expression of cDNA encoding the human 150 kDa oxygen-
regulated protein, ORP150.";
Biochem. Biophys. Res. Commun. 230:94-99(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10965054; DOI=10.1093/oxfordjournals.jbchem.a022783;
Kaneda S., Yura T., Yanagi H.;
"Production of three distinct mRNAs of 150 kDa oxygen-regulated
protein (ORP150) by alternative promoters: preferential induction of
one species under stress conditions.";
J. Biochem. 128:529-538(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=17131193; DOI=10.1007/s10930-006-9038-z;
Takeuchi S.;
"Molecular cloning, sequence, function and structural basis of human
heart 150 kDa oxygen-regulated protein, an ER chaperone.";
Protein J. 25:517-528(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
PROTEIN SEQUENCE OF 241-256; 541-555; 577-594 AND 754-768, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
FUNCTION.
PubMed=10037731; DOI=10.1074/jbc.274.10.6397;
Ozawa K., Kuwabara K., Tamatani M., Takatsuji K., Tsukamoto Y.,
Kaneda S., Yanagi H., Stern D.M., Eguchi Y., Tsujimoto Y., Ogawa S.,
Tohyama M.;
"150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced
apoptotic cell death.";
J. Biol. Chem. 274:6397-6404(1999).
[10]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[11]
GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 AND
ASN-931.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 AND
ASN-931.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830;
ASN-862 AND ASN-931.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER THR-32, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms
triggered by oxygen deprivation. May play a role as a molecular
chaperone and participate in protein folding.
{ECO:0000269|PubMed:10037731}.
-!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
UGT1A1 and very small amounts of ERP29, but not, or at very low
levels, CALR nor CANX.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y4L1-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y4L1-2; Sequence=VSP_056364, VSP_056365, VSP_056366;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in tissues that contain well-
developed endoplasmic reticulum and synthesize large amounts of
secretory proteins. Highly expressed in liver and pancreas and
lower expression in brain and kidney. Also expressed in
macrophages within aortic atherosclerotic plaques, and in breast
cancers.
-!- INDUCTION: By hypoxia and also by 2-deoxyglucose or tunicamycin.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; U65785; AAC50947.1; -; mRNA.
EMBL; AB009979; BAF80348.1; -; Genomic_DNA.
EMBL; DQ350134; ABC75106.1; -; mRNA.
EMBL; DQ372932; ABD14370.1; -; mRNA.
EMBL; AK304264; BAH14145.1; -; mRNA.
EMBL; AK314178; BAG36860.1; -; mRNA.
EMBL; AK222756; BAD96476.1; -; mRNA.
EMBL; EF444986; ACA06002.1; -; Genomic_DNA.
EMBL; AP003392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS8408.1; -. [Q9Y4L1-1]
PIR; JC5278; JC5278.
RefSeq; NP_001124463.1; NM_001130991.2. [Q9Y4L1-1]
RefSeq; NP_006380.1; NM_006389.4. [Q9Y4L1-1]
RefSeq; XP_016872585.1; XM_017017096.1. [Q9Y4L1-1]
RefSeq; XP_016872586.1; XM_017017097.1. [Q9Y4L1-1]
UniGene; Hs.277704; -.
ProteinModelPortal; Q9Y4L1; -.
SMR; Q9Y4L1; -.
BioGrid; 115780; 116.
IntAct; Q9Y4L1; 46.
MINT; Q9Y4L1; -.
STRING; 9606.ENSP00000384144; -.
ChEMBL; CHEMBL2216741; -.
CarbonylDB; Q9Y4L1; -.
iPTMnet; Q9Y4L1; -.
PhosphoSitePlus; Q9Y4L1; -.
SwissPalm; Q9Y4L1; -.
BioMuta; HYOU1; -.
DMDM; 10720185; -.
REPRODUCTION-2DPAGE; IPI00000877; -.
EPD; Q9Y4L1; -.
PaxDb; Q9Y4L1; -.
PeptideAtlas; Q9Y4L1; -.
PRIDE; Q9Y4L1; -.
ProteomicsDB; 86227; -.
Ensembl; ENST00000617285; ENSP00000480150; ENSG00000149428. [Q9Y4L1-1]
Ensembl; ENST00000630669; ENSP00000486825; ENSG00000280682. [Q9Y4L1-1]
GeneID; 10525; -.
KEGG; hsa:10525; -.
UCSC; uc031yhc.2; human. [Q9Y4L1-1]
CTD; 10525; -.
DisGeNET; 10525; -.
EuPathDB; HostDB:ENSG00000149428.18; -.
GeneCards; HYOU1; -.
HGNC; HGNC:16931; HYOU1.
HPA; HPA049296; -.
MIM; 601746; gene.
neXtProt; NX_Q9Y4L1; -.
OpenTargets; ENSG00000149428; -.
PharmGKB; PA38427; -.
eggNOG; KOG0104; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00390000016919; -.
HOGENOM; HOG000007865; -.
HOVERGEN; HBG106402; -.
InParanoid; Q9Y4L1; -.
KO; K09486; -.
OMA; RSLKHNK; -.
OrthoDB; EOG091G025X; -.
PhylomeDB; Q9Y4L1; -.
TreeFam; TF105048; -.
Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
SIGNOR; Q9Y4L1; -.
ChiTaRS; HYOU1; human.
GeneWiki; HYOU1; -.
GenomeRNAi; 10525; -.
PMAP-CutDB; Q9Y4L1; -.
PRO; PR:Q9Y4L1; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149428; Expressed in 230 organ(s), highest expression level in islet of Langerhans.
CleanEx; HS_HYOU1; -.
ExpressionAtlas; Q9Y4L1; baseline and differential.
Genevisible; Q9Y4L1; HS.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; NAS:ParkinsonsUK-UCL.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL.
GO; GO:0071456; P:cellular response to hypoxia; IDA:ParkinsonsUK-UCL.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IDA:ParkinsonsUK-UCL.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:ParkinsonsUK-UCL.
GO; GO:0002931; P:response to ischemia; ISS:ParkinsonsUK-UCL.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Chaperone;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Glycoprotein; Nucleotide-binding; Phosphoprotein; Reference proteome;
Signal; Stress response.
SIGNAL 1 32 {ECO:0000244|PubMed:25944712}.
CHAIN 33 999 Hypoxia up-regulated protein 1.
/FTId=PRO_0000013538.
MOTIF 996 999 Prevents secretion from ER.
{ECO:0000255}.
COMPBIAS 603 606 Poly-Glu.
COMPBIAS 636 641 Poly-Pro.
MOD_RES 567 567 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 883 883 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JKR6}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 596 596 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 830 830 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 862 862 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 869 869 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 922 922 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 931 931 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
VAR_SEQ 1 87 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056364.
VAR_SEQ 603 646 EEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKG
DAT -> MLFLCPARLPQSKQAIDRFHTAVTCMEPPWGRRC
RARPAWRLCS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056365.
VAR_SEQ 647 999 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056366.
CONFLICT 75 75 K -> E (in Ref. 5; BAD96476).
{ECO:0000305}.
CONFLICT 92 92 N -> D (in Ref. 5; BAD96476).
{ECO:0000305}.
CONFLICT 255 255 M -> T (in Ref. 5; BAD96476).
{ECO:0000305}.
CONFLICT 442 442 V -> A (in Ref. 5; BAD96476).
{ECO:0000305}.
SEQUENCE 999 AA; 111335 MW; FCE0F292466AFAB9 CRC64;
MADKVRRQRP RRRVCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF QHLLGKQADN PHVALYQARF
PEHELTFDPQ RQTVHFQISS QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPVFF
NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC
TIVTYQMVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR ERLAGLFNEQ RKGQRAKDVR
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFERVP
GPVQQALQSA EMSLDEIEQV ILVGGATRVP RVQEVLLKAV GKEELGKNIN ADEAAAMGAV
YQAAALSKAF KVKPFVVRDA VVYPILVEFT REVEEEPGIH SLKHNKRVLF SRMGPYPQRK
VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK
AHFNLDESGV LSLDRVESVF ETLVEDSAEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT
VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPPPPE PKGDATPEGE KATEKENGDK
SEAQKPSEKA EAGPEGVAPA PEGEKKQKPA RKRRMVEEIG VELVVLDLPD LPEDKLAQSV
QKLQDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSAAST
WLEDEGVGAT TVMLKEKLAE LRKLCQGLFF RVEERKKWPE RLSALDNLLN HSSMFLKGAR
LIPEMDQIFT EVEMTTLEKV INETWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASASDQGEK VIPPAGQTED AEPISEPEKV
ETGSEPGDTE PLELGGPGAE PEQKEQSTGQ KRPLKNDEL


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CSB-EL020073BO Bovine Oxygen-regulated protein 1(RP1) ELISA kit 96T
CSB-EL020073DO Dog Oxygen-regulated protein 1(RP1) ELISA kit SpeciesDog 96T
CSB-EL020073HU Human Oxygen-regulated protein 1(RP1) ELISA kit 96T
CSB-EL020073MO Mouse Oxygen-regulated protein 1(RP1) ELISA kit 96T
EIAAB05237 Calmodulin-regulated spectrin-associated protein 1-like protein 1,Calmodulin-regulated spectrin-associated protein 2,CAMSAP1L1,CAMSAP2,Homo sapiens,Human,KIAA1078
CSB-EL020073BO Bovine Oxygen-regulated protein 1(RP1) ELISA kit SpeciesBovine 96T
CSB-EL020073MO Mouse Oxygen-regulated protein 1(RP1) ELISA kit SpeciesMouse 96T
CSB-EL020073HU Human Oxygen-regulated protein 1(RP1) ELISA kit SpeciesHuman 96T
HSPA5-332H Protein Recombinant Human Heat Shock 70kDa Protein 5 (Glucose-regulated Protein, 78kDa), His-tagged 20ug
HSPA5-332H Protein: Recombinant Human Heat Shock 70kDa Protein 5 (Glucose-regulated Protein, 78kDa), His-tagged 20ug
EIAAB05236 Calmodulin-regulated spectrin-associated protein 1-like protein 1,Calmodulin-regulated spectrin-associated protein 2,Camsap1l1,Camsap2,Kiaa1078,Mouse,Mus musculus
bs-11030R Rabbit Anti-Oxygen-regulated protein 1 Polyclonal Antibody 100ul
RP1_MOUSE ELISA Kit FOR Oxygen-regulated protein 1; organism: Mouse; gene name: Rp1 96T
HYOU1_HUMAN Human ELISA Kit FOR Hypoxia up-regulated protein 1 96T


 

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