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Uromodulin (Tamm-Horsfall urinary glycoprotein) (THP) [Cleaved into: Uromodulin, secreted form]

 UROM_MOUSE              Reviewed;         642 AA.
Q91X17; Q3TN64; Q3TP60; Q62285;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 137.
RecName: Full=Uromodulin;
AltName: Full=Tamm-Horsfall urinary glycoprotein;
Short=THP;
Contains:
RecName: Full=Uromodulin, secreted form;
Flags: Precursor;
Name=Umod;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7873609; DOI=10.1016/0167-4781(94)00240-4;
Prasadan K., Bates J., Badgett A., Dell M., Sukhatme V., Yu H.,
Kumar S.;
"Nucleotide sequence and peptide motifs of mouse uromodulin (Tamm-
Horsfall protein) -- the most abundant protein in mammalian urine.";
Biochim. Biophys. Acta 1260:328-332(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
GLYCOSYLATION, AND DOMAIN ZP.
PubMed=12021773; DOI=10.1038/ncb802;
Jovine L., Qi H., Williams Z., Litscher E., Wassarman P.M.;
"The ZP domain is a conserved module for polymerization of
extracellular proteins.";
Nat. Cell Biol. 4:457-461(2002).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=14871399; DOI=10.1111/j.1523-1755.2004.00452.x;
Bates J.M., Raffi H.M., Prasadan K., Mascarenhas R., Laszik Z.,
Maeda N., Hultgren S.J., Kumar S.;
"Tamm-Horsfall protein knockout mice are more prone to urinary tract
infection: rapid communication.";
Kidney Int. 65:791-797(2004).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15327412; DOI=10.1111/j.1523-1755.2004.00867.x;
Mo L., Huang H.Y., Zhu X.H., Shapiro E., Hasty D.L., Wu X.R.;
"Tamm-Horsfall protein is a critical renal defense factor protecting
against calcium oxalate crystal formation.";
Kidney Int. 66:1159-1166(2004).
[7]
PROTEIN SEQUENCE OF 573-587, PROTEOLYTIC CLEAVAGE, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18375198; DOI=10.1016/j.bbrc.2008.03.099;
Santambrogio S., Cattaneo A., Bernascone I., Schwend T., Jovine L.,
Bachi A., Rampoldi L.;
"Urinary uromodulin carries an intact ZP domain generated by a
conserved C-terminal proteolytic cleavage.";
Biochem. Biophys. Res. Commun. 370:410-413(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, IDENTIFICATION BY MASS
SPECTROMETRY, TISSUE SPECIFICITY, AND DOMAIN.
PubMed=26673890; DOI=10.7554/eLife.08887;
Brunati M., Perucca S., Han L., Cattaneo A., Consolato F., Andolfo A.,
Schaeffer C., Olinger E., Peng J., Santambrogio S., Perrier R., Li S.,
Bokhove M., Bachi A., Hummler E., Devuyst O., Wu Q., Jovine L.,
Rampoldi L.;
"The serine protease hepsin mediates urinary secretion and
polymerisation of Zona Pellucida domain protein uromodulin.";
Elife 4:0-0(2015).
-!- FUNCTION: Uromodulin: Functions in biogenesis and organization of
the apical membrane of epithelial cells of the thick ascending
limb of Henle's loop (TALH), where it promotes formation of
complex filamentous gel-like structure that may play a role in the
water barrier permeability. May serve as a receptor for binding
and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates
neutrophil migration across renal epithelia.
{ECO:0000250|UniProtKB:P07911}.
-!- FUNCTION: Uromodulin, secreted form: In the urine, may contribute
to colloid osmotic pressure, retards passage of positively charged
electrolytes, prevents urinary tract infection and inhibits
formation of liquid containing supersaturated salts and subsequent
formation of salt crystals. {ECO:0000269|PubMed:14871399,
ECO:0000269|PubMed:15327412}.
-!- SUBUNIT: Uromodulin, secreted form: homodimer that then
polymerizes into long filaments. {ECO:0000269|PubMed:26673890}.
-!- SUBCELLULAR LOCATION: Uromodulin, secreted form: Secreted
{ECO:0000269|PubMed:26673890}. Note=Detected in urine.
{ECO:0000269|PubMed:26673890}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:26673890}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P07911}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P07911}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P07911}. Cell projection, cilium membrane
{ECO:0000250|UniProtKB:P07911}. Note=Only a small fraction sorts
to the basolateral pole of tubular epithelial cells compared to
apical localization. Secreted into urine after cleavage.
Colocalizes with NPHP1 and KIF3A. {ECO:0000250|UniProtKB:P07911}.
-!- TISSUE SPECIFICITY: Detected in urine (secreted form). Detected in
kidney thick ascending limb epithelial cells (at protein level).
{ECO:0000269|PubMed:26673890}.
-!- DOMAIN: The ZP domain mediates polymerization, leading to the
formation of long filaments. {ECO:0000269|PubMed:12021773,
ECO:0000269|PubMed:26673890}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12021773,
ECO:0000269|PubMed:26673890}.
-!- PTM: Proteolytically cleaved at a conserved C-terminal proteolytic
cleavage site to generate the secreted form found in urine
(PubMed:18375198). This cleavage is catalyzed by HPN
(PubMed:26673890). {ECO:0000269|PubMed:18375198,
ECO:0000269|PubMed:26673890}.
-!- DISRUPTION PHENOTYPE: Mice suffer significantly more frequently
from urinary tract infections. They shown also spontaneous
formation of calcium crystals in adult kidneys, and excessive
intake of calcium and oxalate dramatically increases both the
frequency and the severity of renal calcium crystal formation in
mutant mice, but not in wild-type mice.
{ECO:0000269|PubMed:14871399, ECO:0000269|PubMed:15327412}.
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EMBL; L33406; AAA73896.1; -; mRNA.
EMBL; AK085460; BAC39452.1; -; mRNA.
EMBL; AK144065; BAE25681.1; -; mRNA.
EMBL; AK164688; BAE37877.1; -; mRNA.
EMBL; AK165507; BAE38225.1; -; mRNA.
EMBL; BC012973; AAH12973.1; -; mRNA.
CCDS; CCDS21780.1; -.
PIR; S52111; S52111.
RefSeq; NP_001265534.1; NM_001278605.1.
RefSeq; NP_033496.1; NM_009470.5.
UniGene; Mm.10826; -.
ProteinModelPortal; Q91X17; -.
SMR; Q91X17; -.
STRING; 10090.ENSMUSP00000033263; -.
iPTMnet; Q91X17; -.
PhosphoSitePlus; Q91X17; -.
MaxQB; Q91X17; -.
PaxDb; Q91X17; -.
PRIDE; Q91X17; -.
Ensembl; ENSMUST00000033263; ENSMUSP00000033263; ENSMUSG00000030963.
Ensembl; ENSMUST00000209095; ENSMUSP00000146652; ENSMUSG00000030963.
GeneID; 22242; -.
KEGG; mmu:22242; -.
UCSC; uc009jlb.2; mouse.
CTD; 7369; -.
MGI; MGI:102674; Umod.
eggNOG; ENOG410IVSV; Eukaryota.
eggNOG; ENOG410YDU6; LUCA.
GeneTree; ENSGT00530000063244; -.
HOGENOM; HOG000293303; -.
HOVERGEN; HBG004349; -.
InParanoid; Q91X17; -.
KO; K18274; -.
OMA; GPCGTVM; -.
OrthoDB; EOG091G06RJ; -.
PhylomeDB; Q91X17; -.
TreeFam; TF330284; -.
Reactome; R-MMU-446203; Asparagine N-linked glycosylation.
ChiTaRS; Umod; mouse.
PRO; PR:Q91X17; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030963; -.
CleanEx; MM_UMOD; -.
ExpressionAtlas; Q91X17; baseline and differential.
Genevisible; Q91X17; MM.
GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0019864; F:IgG binding; ISO:MGI.
GO; GO:0048878; P:chemical homeostasis; IMP:MGI.
GO; GO:0007588; P:excretion; IMP:MGI.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
GO; GO:0072218; P:metanephric ascending thin limb development; IEP:UniProtKB.
GO; GO:0072221; P:metanephric distal convoluted tubule development; IEP:UniProtKB.
GO; GO:0072233; P:metanephric thick ascending limb development; IEP:UniProtKB.
GO; GO:1990266; P:neutrophil migration; ISO:MGI.
GO; GO:2000021; P:regulation of ion homeostasis; IMP:UniProtKB.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR024731; EGF_dom.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001507; ZP_dom.
InterPro; IPR017977; ZP_dom_CS.
Pfam; PF12947; EGF_3; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00023; ZPELLUCIDA.
SMART; SM00181; EGF; 3.
SMART; SM00179; EGF_CA; 2.
SMART; SM00241; ZP; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 3.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS00682; ZP_1; 1.
PROSITE; PS51034; ZP_2; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 24 {ECO:0000250|UniProtKB:P07911}.
CHAIN 25 618 Uromodulin.
/FTId=PRO_0000041673.
CHAIN 25 588 Uromodulin, secreted form.
/FTId=PRO_0000407910.
PROPEP 619 642 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000041674.
DOMAIN 28 64 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 65 106 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 107 148 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 335 590 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
REGION 431 454 Important for secretion and
polymerization into filaments.
{ECO:0000250|UniProtKB:P07911}.
REGION 587 590 Essential for cleavage by HPN.
{ECO:0000250|UniProtKB:P07911}.
REGION 599 608 Regulates polymerization into filaments.
{ECO:0000250|UniProtKB:P07911}.
SITE 588 589 Cleavage. {ECO:0000269|PubMed:18375198,
ECO:0000269|PubMed:26673890}.
LIPID 618 618 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 514 514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 41 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 35 50 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 52 63 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 69 82 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 77 91 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 93 105 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 111 125 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 119 134 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 136 147 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 298 307 {ECO:0000250|UniProtKB:P07911}.
DISULFID 301 316 {ECO:0000250|UniProtKB:P07911}.
DISULFID 318 348 {ECO:0000250|UniProtKB:P07911}.
DISULFID 336 426 {ECO:0000250|UniProtKB:P07911}.
DISULFID 367 390 {ECO:0000250|UniProtKB:P07911}.
DISULFID 507 567 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 528 583 {ECO:0000250|UniProtKB:P07911}.
DISULFID 572 579 {ECO:0000250|UniProtKB:P07911}.
CONFLICT 22 22 E -> G (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 102 104 ELS -> GLG (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 138 138 E -> K (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 152 152 G -> S (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 200 200 L -> Q (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 223 223 R -> A (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 255 255 Q -> H (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 279 279 A -> E (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 340 340 D -> G (in Ref. 2; BAE38225).
{ECO:0000305}.
CONFLICT 473 473 H -> Y (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 590 590 S -> C (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 606 606 T -> TRQ (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 616 617 Missing (in Ref. 1; AAA73896).
{ECO:0000305}.
CONFLICT 633 633 P -> L (in Ref. 1; AAA73896).
{ECO:0000305}.
SEQUENCE 642 AA; 70845 MW; 31B1461B4DCAE927 CRC64;
MGIPLTWMLL VMMVTSWFTL AEASNSTEAR RCSECHNNAT CTVDGVVTTC SCQTGFTGDG
LVCEDMDECA TPWTHNCSNS SCVNTPGSFK CSCQDGFRLT PELSCTDVDE CSEQGLSNCH
ALATCVNTEG DYLCVCPEGF TGDGWYCECS PGSCEPGLDC LPQGPDGKLV CQDPCNTYET
LTEYWRSTEY GVGYSCDAGL HGWYRFTGQG GVRMAETCVP VLRCNTAAPM WLNGSHPSSS
EGIVSRTACA HWSDQCCRWS TEIQVKACPG GFYIYNLTAP PECNLAYCTD PSSVEGTCEE
CRVDEDCISD NGRWRCQCKQ DSNITDVSQL EYRLECGAND IKMSLRKCQL QSLGFMNVFM
YLNDRQCSGF SESDERDWMS IVTPARNGPC GTVLRRNETH ATYSNTLYLA NAIIIRDIII
RMNFECSYPL DMKVSLKTSL QPMVSALNIS LGGTGKFTVR MALFQSPTYT QPHQGPSVML
STEAFLYVGT MLDGGDLSRF VLLMTNCYAT PSSNSTDPVK YFIIQDSCPR TEDTTIQVTE
NGESSQARFS VQMFRFAGNY DLVYLHCEVY LCDSTSEQCK PTCSGTRFRS GNFIDQTRVL
NLGPITRQGV QASVSKAASS NLRLLSIWLL LFPSATLIFM VQ


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52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur