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High osmolarity signaling protein SHO1 (Osmosensor SHO1) (Suppressor of SUA8-1 mutation) (Synthetic high osmolarity-sensitive protein 1)

 SHO1_YEAST              Reviewed;         367 AA.
P40073; D3DM24;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
27-SEP-2017, entry version 151.
RecName: Full=High osmolarity signaling protein SHO1;
AltName: Full=Osmosensor SHO1;
AltName: Full=Suppressor of SUA8-1 mutation;
AltName: Full=Synthetic high osmolarity-sensitive protein 1;
Name=SHO1; Synonyms=SSU81; OrderedLocusNames=YER118C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Berroteran R.W., Hampsey M.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=7624781; DOI=10.1126/science.7624781;
Maeda T., Takekawa M., Saito H.;
"Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-
containing osmosensor.";
Science 269:554-558(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, AND INTERACTION WITH PBS2.
PubMed=9180081; DOI=10.1126/science.276.5319.1702;
Posas F., Saito H.;
"Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK:
scaffold role of Pbs2p MAPKK.";
Science 276:1702-1705(1997).
[6]
FUNCTION.
PubMed=9744864; DOI=10.1101/gad.12.18.2874;
O'Rourke S.M., Herskowitz I.;
"The Hog1 MAPK prevents cross talk between the HOG and pheromone
response MAPK pathways in Saccharomyces cerevisiae.";
Genes Dev. 12:2874-2886(1998).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PBS2.
PubMed=10970855; DOI=10.1093/emboj/19.17.4623;
Raitt D.C., Posas F., Saito H.;
"Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent
activation of the Hog1 MAPK pathway.";
EMBO J. 19:4623-4631(2000).
[8]
FUNCTION.
PubMed=11084293; DOI=10.1016/S0891-5849(00)00432-9;
Singh K.K.;
"The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system
mediates response to oxidative stress and in an oxidant-specific
fashion.";
Free Radic. Biol. Med. 29:1043-1050(2000).
[9]
FUNCTION.
PubMed=10762242; DOI=10.1128/JB.182.9.2428-2437.2000;
Garcia-Rodriguez L.J., Duran A., Roncero C.;
"Calcofluor antifungal action depends on chitin and a functional high-
osmolarity glycerol response (HOG) pathway: evidence for a
physiological role of the Saccharomyces cerevisiae HOG pathway under
noninducing conditions.";
J. Bacteriol. 182:2428-2437(2000).
[10]
FUNCTION.
PubMed=10931333; DOI=10.1046/j.1365-2958.2000.02002.x;
Van Wuytswinkel O., Reiser V., Siderius M., Kelders M.C., Ammerer G.,
Ruis H., Mager W.H.;
"Response of Saccharomyces cerevisiae to severe osmotic stress:
evidence for a novel activation mechanism of the HOG MAP kinase
pathway.";
Mol. Microbiol. 37:382-397(2000).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10980703; DOI=10.1038/35023568;
Reiser V., Salah S.M., Ammerer G.;
"Polarized localization of yeast Pbs2 depends on osmostress, the
membrane protein Sho1 and Cdc42.";
Nat. Cell Biol. 2:620-627(2000).
[12]
FUNCTION.
PubMed=11922108; DOI=10.1266/ggs.76.393;
Toh-e A., Oguchi T.;
"Defects in glycosylphosphatidylinositol (GPI) anchor synthesis
activate Hog1 kinase and confer copper-resistance in Saccharomyces
cerevisisae.";
Genes Genet. Syst. 76:393-410(2001).
[13]
FUNCTION.
PubMed=12455951; DOI=10.1128/EC.1.2.163-173.2002;
Winkler A., Arkind C., Mattison C.P., Burkholder A., Knoche K.,
Ota I.M.;
"Heat stress activates the yeast high-osmolarity glycerol mitogen-
activated protein kinase pathway, and protein tyrosine phosphatases
are essential under heat stress.";
Eukaryot. Cell 1:163-173(2002).
[14]
SUBCELLULAR LOCATION.
PubMed=12374868; DOI=10.1073/pnas.172517799;
Bagnat M., Simons K.;
"Cell surface polarization during yeast mating.";
Proc. Natl. Acad. Sci. U.S.A. 99:14183-14188(2002).
[15]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[16]
DOMAIN, AND INTERACTION WITH PBS2.
PubMed=14668868; DOI=10.1038/nature02178;
Zarrinpar A., Park S.H., Lim W.A.;
"Optimization of specificity in a cellular protein interaction network
by negative selection.";
Nature 426:676-680(2003).
[17]
FUNCTION.
PubMed=12511654; DOI=10.1126/science.1076979;
Park S.H., Zarrinpar A., Lim W.A.;
"Rewiring MAP kinase pathways using alternative scaffold assembly
mechanisms.";
Science 299:1061-1064(2003).
[18]
FUNCTION, AND INTERACTION WITH MSB2.
PubMed=15256499; DOI=10.1101/gad.1178604;
Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K.,
Neal C., Delrow J., Bardwell L., Sprague G.F. Jr.;
"A signaling mucin at the head of the Cdc42- and MAPK-dependent
filamentous growth pathway in yeast.";
Genes Dev. 18:1695-1708(2004).
[19]
FUNCTION, AND INTERACTION WITH FUS1.
PubMed=15020407; DOI=10.1534/genetics.166.1.67;
Nelson B., Parsons A.B., Evangelista M., Schaefer K., Kennedy K.,
Ritchie S., Petryshen T.L., Boone C.;
"Fus1p interacts with components of the Hog1p mitogen-activated
protein kinase and Cdc42p morphogenesis signaling pathways to control
cell fusion during yeast mating.";
Genetics 166:67-77(2004).
[20]
FUNCTION.
PubMed=14595107; DOI=10.1091/mbc.E03-07-0521;
O'Rourke S.M., Herskowitz I.;
"Unique and redundant roles for HOG MAPK pathway components as
revealed by whole-genome expression analysis.";
Mol. Biol. Cell 15:532-542(2004).
[21]
FUNCTION, INTERACTION WITH PBS2, DOMAIN, AND MUTAGENESIS OF TYR-309;
ASP-317 AND TYR-355.
PubMed=15200958; DOI=10.1016/j.molcel.2004.05.024;
Marles J.A., Dahesh S., Haynes J., Andrews B.J., Davidson A.R.;
"Protein-protein interaction affinity plays a crucial role in
controlling the Sho1p-mediated signal transduction pathway in yeast.";
Mol. Cell 14:813-823(2004).
[22]
FUNCTION, AND INTERACTION WITH STE11.
PubMed=15200959; DOI=10.1016/j.molcel.2004.06.011;
Zarrinpar A., Bhattacharyya R.P., Nittler M.P., Lim W.A.;
"Sho1 and Pbs2 act as coscaffolds linking components in the yeast high
osmolarity MAP kinase pathway.";
Mol. Cell 14:825-832(2004).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[24]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STE11 AND STE50.
PubMed=16778768; DOI=10.1038/sj.emboj.7601192;
Tatebayashi K., Yamamoto K., Tanaka K., Tomida T., Maruoka T.,
Kasukawa E., Saito H.;
"Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast
osmoregulatory HOG MAPK pathway.";
EMBO J. 25:3033-3044(2006).
[25]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[26]
PHOSPHORYLATION AT SER-166, MUTAGENESIS OF SER-166, AND SUBUNIT.
PubMed=17363249; DOI=10.1016/j.cub.2007.02.044;
Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H.,
Elston T.C., Dohlman H.G.;
"A systems-biology analysis of feedback inhibition in the Sho1
osmotic-stress-response pathway.";
Curr. Biol. 17:659-667(2007).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[28]
FUNCTION.
PubMed=18480263; DOI=10.1073/pnas.0710770105;
Hersen P., McClean M.N., Mahadevan L., Ramanathan S.;
"Signal processing by the HOG MAP kinase pathway.";
Proc. Natl. Acad. Sci. U.S.A. 105:7165-7170(2008).
[29]
FUNCTION.
PubMed=19439450; DOI=10.1091/mbc.E08-07-0760;
Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J.;
"The signaling mucins Msb2 and Hkr1 differentially regulate the
filamentation mitogen-activated protein kinase pathway and contribute
to a multimodal response.";
Mol. Biol. Cell 20:3101-3114(2009).
[30]
FUNCTION.
PubMed=19318625; DOI=10.1126/scisignal.2000056;
Macia J., Regot S., Peeters T., Conde N., Sole R., Posas F.;
"Dynamic signaling in the Hog1 MAPK pathway relies on high basal
signal transduction.";
Sci. Signal. 2:RA13-RA13(2009).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[32]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 298-367.
Kursula P., Kursula I., Song Y.H., Paraskevopoulos M., Wilmanns M.;
"Structural genomics of yeast SH3 domains.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Plasma membrane osmosensor that activates the high
osmolarity glycerol (HOG) MAPK signaling pathway in response to
high osmolarity. Detects changes in external osmolarity and
activates PBS2 through the stimulation of STE11 and targets PBS2
to the plasma membrane. PBS2 activation leads to changes in
glycerol production that helps to balance the intracellular and
external osmotic pressures. Activates also HOG1 in response to
heat stress and mediates resistance to oxidative stress. Involved
in the regulation of the mating pathway. May be a receptor that
feeds into the pseudohyphal growth pathway.
{ECO:0000269|PubMed:10762242, ECO:0000269|PubMed:10931333,
ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:10980703,
ECO:0000269|PubMed:11084293, ECO:0000269|PubMed:11922108,
ECO:0000269|PubMed:12455951, ECO:0000269|PubMed:12511654,
ECO:0000269|PubMed:14595107, ECO:0000269|PubMed:15020407,
ECO:0000269|PubMed:15200958, ECO:0000269|PubMed:15200959,
ECO:0000269|PubMed:15256499, ECO:0000269|PubMed:16778768,
ECO:0000269|PubMed:18480263, ECO:0000269|PubMed:19318625,
ECO:0000269|PubMed:19439450, ECO:0000269|PubMed:7624781,
ECO:0000269|PubMed:9180081, ECO:0000269|PubMed:9744864}.
-!- SUBUNIT: Forms homooligomers. Interacts (via the SH3 domain) with
PBS2. Interacts with FUS1, STE11, STE50 and RNA polymerase II.
{ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:14668868,
ECO:0000269|PubMed:15020407, ECO:0000269|PubMed:15200958,
ECO:0000269|PubMed:15200959, ECO:0000269|PubMed:15256499,
ECO:0000269|PubMed:16778768, ECO:0000269|PubMed:17363249,
ECO:0000269|PubMed:9180081}.
-!- INTERACTION:
P42884:AAD14; NbExp=2; IntAct=EBI-18140, EBI-1994;
P36122:BCH2; NbExp=2; IntAct=EBI-18140, EBI-26374;
Q07533:CYK3; NbExp=4; IntAct=EBI-18140, EBI-31510;
P11710:FUS1; NbExp=8; IntAct=EBI-18140, EBI-7179;
P40036:GIP2; NbExp=2; IntAct=EBI-18140, EBI-7612;
Q05080:HOF1; NbExp=5; IntAct=EBI-18140, EBI-5412;
P53901:INN1; NbExp=4; IntAct=EBI-18140, EBI-28955;
Q12446:LAS17; NbExp=10; IntAct=EBI-18140, EBI-10022;
P53153:LCL3; NbExp=2; IntAct=EBI-18140, EBI-23857;
P21339:MSB1; NbExp=2; IntAct=EBI-18140, EBI-11322;
P08018:PBS2; NbExp=7; IntAct=EBI-18140, EBI-12972;
P39081:PCF11; NbExp=2; IntAct=EBI-18140, EBI-12980;
P39083:RGA1; NbExp=2; IntAct=EBI-18140, EBI-15044;
P23561:STE11; NbExp=3; IntAct=EBI-18140, EBI-18259;
P25344:STE50; NbExp=3; IntAct=EBI-18140, EBI-18305;
Q06412:TUS1; NbExp=3; IntAct=EBI-18140, EBI-37117;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Bud. Bud neck. Cell projection. Note=Localizes at the tip of the
mating projection during conjugation.
-!- MISCELLANEOUS: Present with 2330 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U15653; AAA61904.1; -; Genomic_DNA.
EMBL; L41926; AAC41664.1; -; Genomic_DNA.
EMBL; U18916; AAC03216.1; -; Genomic_DNA.
EMBL; BK006939; DAA07778.1; -; Genomic_DNA.
PIR; S50621; S50621.
RefSeq; NP_011043.1; NM_001179008.1.
PDB; 2VKN; X-ray; 2.05 A; A=298-367.
PDBsum; 2VKN; -.
ProteinModelPortal; P40073; -.
SMR; P40073; -.
BioGrid; 36863; 180.
DIP; DIP-2472N; -.
IntAct; P40073; 81.
MINT; MINT-518897; -.
STRING; 4932.YER118C; -.
iPTMnet; P40073; -.
PRIDE; P40073; -.
EnsemblFungi; YER118C; YER118C; YER118C.
GeneID; 856854; -.
KEGG; sce:YER118C; -.
EuPathDB; FungiDB:YER118C; -.
SGD; S000000920; SHO1.
HOGENOM; HOG000174182; -.
InParanoid; P40073; -.
KO; K11246; -.
OMA; WFAIFLQ; -.
OrthoDB; EOG092C3BG5; -.
BioCyc; YEAST:G3O-30282-MONOMER; -.
EvolutionaryTrace; P40073; -.
PRO; PR:P40073; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0005933; C:cellular bud; IDA:SGD.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0044697; C:HICS complex; IPI:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043332; C:mating projection tip; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:SGD.
GO; GO:0005034; F:osmosensor activity; IPI:SGD.
GO; GO:0034605; P:cellular response to heat; IMP:SGD.
GO; GO:0030010; P:establishment of cell polarity; IGI:SGD.
GO; GO:0007231; P:osmosensory signaling pathway; IGI:SGD.
GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
CDD; cd11855; SH3_Sho1p; 1.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035522; Sho1_SH3.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Complete proteome;
Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
SH3 domain; Stress response; Transmembrane; Transmembrane helix.
CHAIN 1 367 High osmolarity signaling protein SHO1.
/FTId=PRO_0000072231.
TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.
TRANSMEM 33 53 Helical. {ECO:0000255}.
TOPO_DOM 54 65 Extracellular. {ECO:0000255}.
TRANSMEM 66 86 Helical. {ECO:0000255}.
TOPO_DOM 87 93 Cytoplasmic. {ECO:0000255}.
TRANSMEM 94 114 Helical. {ECO:0000255}.
TOPO_DOM 115 122 Extracellular. {ECO:0000255}.
TRANSMEM 123 143 Helical. {ECO:0000255}.
TOPO_DOM 144 367 Cytoplasmic. {ECO:0000255}.
DOMAIN 300 361 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000269|PubMed:17363249}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 166 166 S->E: Diminishes the formation of
oligomers, dampens activation of the HOG1
kinase, and impairs growth in high-salt
or sorbitol conditions.
{ECO:0000269|PubMed:17363249}.
MUTAGEN 309 309 Y->A: Decreases the interaction with PBS2
and leads to decreased HOG pathway
response and increased aberrant mating
pathway activation.
{ECO:0000269|PubMed:15200958}.
MUTAGEN 317 317 D->I,H: Decreases the interaction with
PBS2 and leads to decreased HOG pathway
response and increased aberrant mating
pathway activation.
{ECO:0000269|PubMed:15200958}.
MUTAGEN 355 355 Y->A,F,I,M: Decreases the interaction
with PBS2 and leads to decreased HOG
pathway response and increased aberrant
mating pathway activation.
{ECO:0000269|PubMed:15200958}.
STRAND 302 309 {ECO:0000244|PDB:2VKN}.
STRAND 315 317 {ECO:0000244|PDB:2VKN}.
STRAND 328 332 {ECO:0000244|PDB:2VKN}.
STRAND 336 342 {ECO:0000244|PDB:2VKN}.
STRAND 348 352 {ECO:0000244|PDB:2VKN}.
HELIX 353 355 {ECO:0000244|PDB:2VKN}.
STRAND 356 363 {ECO:0000244|PDB:2VKN}.
SEQUENCE 367 AA; 41126 MW; E467A4D50AA3EDB6 CRC64;
MSISSKIRPT PRKPSRMATD HSFKMKKFYA DPFAISSISL AIVSWVIAIG GSISSASTNE
SFPRFTWWGI VYQFLIICSL MLFYCFDLVD HYRIFITTSI AVAFVYNTNS ATNLVYADGP
KKAAASAGVI LLSIINLIWI LYYGGDNASP TNRWIDSFSI KGIRPSPLEN SLHRARRRGN
RNTTPYQNNV YNDAIRDSGY ATQFDGYPQQ QPSHTNYVSS TALAGFENTQ PNTSEAVNLH
LNTLQQRINS ASNAKETNDN SNNQTNTNIG NTFDTDFSNG NTETTMGDTL GLYSDIGDDN
FIYKAKALYP YDADDDDAYE ISFEQNEILQ VSDIEGRWWK ARRANGETGI IPSNYVQLID
GPEEMHR


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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