Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ferric/cupric reductase transmembrane component 1 (EC 1.16.1.9) (Ferric-chelate reductase 1)

 FRE1_YEAST              Reviewed;         686 AA.
P32791; D6VYL5;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
10-OCT-2018, entry version 157.
RecName: Full=Ferric/cupric reductase transmembrane component 1 {ECO:0000305};
EC=1.16.1.9 {ECO:0000269|PubMed:11120744, ECO:0000269|PubMed:1431884, ECO:0000269|PubMed:15288128, ECO:0000269|PubMed:8662826, ECO:0000269|PubMed:8662973};
AltName: Full=Ferric-chelate reductase 1 {ECO:0000305};
Flags: Precursor;
Name=FRE1; OrderedLocusNames=YLR214W; ORFNames=L8167.2;
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], FUNCTION, AND INDUCTION.
STRAIN=F113;
PubMed=1570306; DOI=10.1073/pnas.89.9.3869;
Dancis A., Roman D.G., Anderson G.J., Hinnebusch A.G., Klausner R.D.;
"Ferric reductase of Saccharomyces cerevisiae: molecular
characterization, role in iron uptake, and transcriptional control by
iron.";
Proc. Natl. Acad. Sci. U.S.A. 89:3869-3873(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
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).
[4]
FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=1431884; DOI=10.1016/0162-0134(92)84070-4;
Anderson G.J., Lesuisse E., Dancis A., Roman D.G., Labbe P.,
Klausner R.D.;
"Ferric iron reduction and iron assimilation in Saccharomyces
cerevisiae.";
J. Inorg. Biochem. 47:249-255(1992).
[5]
INDUCTION.
PubMed=7720713;
Yamaguchi-Iwai Y., Dancis A., Klausner R.D.;
"AFT1: a mediator of iron regulated transcriptional control in
Saccharomyces cerevisiae.";
EMBO J. 14:1231-1239(1995).
[6]
FUNCTION, AND INDUCTION.
PubMed=7814363; DOI=10.1074/jbc.270.1.128;
Hassett R., Kosman D.J.;
"Evidence for Cu(II) reduction as a component of copper uptake by
Saccharomyces cerevisiae.";
J. Biol. Chem. 270:128-134(1995).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=8662826; DOI=10.1074/jbc.271.23.13578;
Lesuisse E., Casteras-Simon M., Labbe P.;
"Evidence for the Saccharomyces cerevisiae ferrireductase system being
a multicomponent electron transport chain.";
J. Biol. Chem. 271:13578-13583(1996).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=8662973; DOI=10.1074/jbc.271.24.14240;
Shatwell K.P., Dancis A., Cross A.R., Klausner R.D., Segal A.W.;
"The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome
b similar to that of NADPH oxidase.";
J. Biol. Chem. 271:14240-14244(1996).
[9]
HEME BINDING, AND MUTAGENESIS OF HIS-294; HIS-308; HIS-364 AND
HIS-378.
PubMed=8940093; DOI=10.1074/jbc.271.49.31021;
Finegold A.A., Shatwell K.P., Segal A.W., Klausner R.D., Dancis A.;
"Intramembrane bis-heme motif for transmembrane electron transport
conserved in a yeast iron reductase and the human NADPH oxidase.";
J. Biol. Chem. 271:31021-31024(1996).
[10]
FUNCTION, AND INDUCTION.
PubMed=9153234; DOI=10.1074/jbc.272.21.13786;
Georgatsou E., Mavrogiannis L.A., Fragiadakis G.S., Alexandraki D.;
"The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and
are regulated by the copper-modulated Mac1p activator.";
J. Biol. Chem. 272:13786-13792(1997).
[11]
INDUCTION.
PubMed=9200812;
DOI=10.1002/(SICI)1097-0061(19970615)13:7<621::AID-YEA121>3.3.CO;2-L;
Casas C., Aldea M., Espinet C., Gallego C., Gil R., Herrero E.;
"The AFT1 transcriptional factor is differentially required for
expression of high-affinity iron uptake genes in Saccharomyces
cerevisiae.";
Yeast 13:621-637(1997).
[12]
INDUCTION.
PubMed=9726978; DOI=10.1074/jbc.273.37.23716;
Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
"Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces
cerevisiae.";
J. Biol. Chem. 273:23716-23721(1998).
[13]
ERRATUM.
Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
J. Biol. Chem. 273:30056-30056(1998).
[14]
INDUCTION.
PubMed=10341420;
DOI=10.1002/(SICI)1097-0061(199905)15:7<573::AID-YEA404>3.3.CO;2-Z;
Georgatsou E., Alexandraki D.;
"Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p
Fe/Cu reductase related genes.";
Yeast 15:573-584(1999).
[15]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=11120744; DOI=10.1074/jbc.M010065200;
Yun C.-W., Bauler M., Moore R.E., Klebba P.E., Philpott C.C.;
"The role of the FRE family of plasma membrane reductases in the
uptake of siderophore-iron in Saccharomyces cerevisiae.";
J. Biol. Chem. 276:10218-10223(2001).
[16]
FUNCTION.
PubMed=12954629; DOI=10.1074/jbc.M307019200;
Shi X., Stoj C., Romeo A., Kosman D.J., Zhu Z.;
"Fre1p Cu2+ reduction and Fet3p Cu1+ oxidation modulate copper
toxicity in Saccharomyces cerevisiae.";
J. Biol. Chem. 278:50309-50315(2003).
[17]
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).
[18]
CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
PubMed=15288128; DOI=10.1016/j.freeradbiomed.2004.05.031;
Shinyashiki M., Pan C.J., Lopez B.E., Fukuto J.M.;
"Inhibition of the yeast metal reductase heme protein fre1 by nitric
oxide (NO): a model for inhibition of NADPH oxidase by NO.";
Free Radic. Biol. Med. 37:713-723(2004).
[19]
BIOTECHNOLOGY.
PubMed=16000801; DOI=10.1128/AEM.71.7.3882-3888.2005;
Ramalho P.A., Paiva S., Cavaco-Paulo A., Casal M., Cardoso M.H.,
Ramalho M.T.;
"Azo reductase activity of intact Saccharomyces cerevisiae cells is
dependent on the Fre1p component of plasma membrane ferric
reductase.";
Appl. Environ. Microbiol. 71:3882-3888(2005).
[20]
INDUCTION BY AFT1.
PubMed=16024809; DOI=10.1128/MCB.25.15.6760-6771.2005;
Courel M., Lallet S., Camadro J.-M., Blaiseau P.-L.;
"Direct activation of genes involved in intracellular iron use by the
yeast iron-responsive transcription factor Aft2 without its paralog
Aft1.";
Mol. Cell. Biol. 25:6760-6771(2005).
[21]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17507646; DOI=10.1091/mbc.E07-03-0274;
Aronova S., Wedaman K., Anderson S., Yates J.R. III, Powers T.;
"Probing the membrane environment of the TOR kinases reveals
functional interactions between TORC1, actin, and membrane trafficking
in Saccharomyces cerevisiae.";
Mol. Biol. Cell 18:2779-2794(2007).
-!- FUNCTION: Metalloreductase responsible for reducing extracellular
iron and copper prior to import. Catalyzes the reductive uptake of
Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate
siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates
from the siderophore and can be imported by the high-affinity
Fe(2+) transport complex in the plasma membrane. Also participates
in Cu(2+) reduction and Cu(+) uptake.
{ECO:0000269|PubMed:11120744, ECO:0000269|PubMed:12954629,
ECO:0000269|PubMed:1431884, ECO:0000269|PubMed:1570306,
ECO:0000269|PubMed:7814363, ECO:0000269|PubMed:8662826,
ECO:0000269|PubMed:8662973, ECO:0000269|PubMed:9153234}.
-!- CATALYTIC ACTIVITY: 2 Fe(II)-siderophore + NADP(+) + H(+) = 2
Fe(III)-siderophore + NADPH. {ECO:0000269|PubMed:11120744,
ECO:0000269|PubMed:1431884, ECO:0000269|PubMed:15288128,
ECO:0000269|PubMed:8662826, ECO:0000269|PubMed:8662973}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:8662973};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:8940093};
-!- ACTIVITY REGULATION: Inhibited by nitric oxide (NO).
{ECO:0000269|PubMed:15288128}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1431884,
ECO:0000269|PubMed:15288128, ECO:0000269|PubMed:17507646,
ECO:0000269|PubMed:8662826}; Multi-pass membrane protein
{ECO:0000255}.
-!- INDUCTION: Expression is repressed by the addition of iron
(PubMed:1570306, PubMed:1431884). Induced by transcription factor
MAC1 upon copper deprivation (PubMed:7814363, PubMed:9153234,
PubMed:9726978, PubMed:10341420). Induced by transcription factor
AFT1 upon iron deprivation (PubMed:7720713, PubMed:9200812,
PubMed:9726978, PubMed:10341420, PubMed:16024809).
{ECO:0000269|PubMed:10341420, ECO:0000269|PubMed:1431884,
ECO:0000269|PubMed:1570306, ECO:0000269|PubMed:16024809,
ECO:0000269|PubMed:7720713, ECO:0000269|PubMed:7814363,
ECO:0000269|PubMed:9153234, ECO:0000269|PubMed:9200812,
ECO:0000269|PubMed:9726978}.
-!- BIOTECHNOLOGY: Responsible for the reduction of the azo bond of
azo dyes, making yeasts efficient azo dye decolorizers.
{ECO:0000269|PubMed:16000801}.
-!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M86908; AAA34608.1; -; Genomic_DNA.
EMBL; U14913; AAB67424.1; -; Genomic_DNA.
EMBL; BK006945; DAA09531.1; -; Genomic_DNA.
PIR; S30075; S30075.
RefSeq; NP_013315.1; NM_001182101.1.
ProteinModelPortal; P32791; -.
SMR; P32791; -.
BioGrid; 31482; 75.
DIP; DIP-5349N; -.
IntAct; P32791; 1.
MINT; P32791; -.
STRING; 4932.YLR214W; -.
TCDB; 5.B.1.5.1; the phagocyte (gp91(phox)) nadph oxidase family.
MaxQB; P32791; -.
PaxDb; P32791; -.
PRIDE; P32791; -.
EnsemblFungi; YLR214W; YLR214W; YLR214W.
GeneID; 850911; -.
KEGG; sce:YLR214W; -.
EuPathDB; FungiDB:YLR214W; -.
SGD; S000004204; FRE1.
GeneTree; ENSGT00390000007891; -.
HOGENOM; HOG000001131; -.
InParanoid; P32791; -.
OMA; WSITESS; -.
OrthoDB; EOG092C2ISR; -.
BioCyc; YEAST:YLR214W-MONOMER; -.
PRO; PR:P32791; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0000293; F:ferric-chelate reductase activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
GO; GO:0015677; P:copper ion import; IDA:SGD.
GO; GO:0006826; P:iron ion transport; IDA:SGD.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR039261; FNR_nucleotide-bd.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
SUPFAM; SSF52343; SSF52343; 2.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Copper; Copper transport;
Electron transport; FAD; Flavoprotein; Glycoprotein; Heme;
Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP;
Oxidoreductase; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 686 Ferric/cupric reductase transmembrane
component 1.
/FTId=PRO_0000010137.
TOPO_DOM 23 148 Extracellular. {ECO:0000255}.
TRANSMEM 149 169 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 170 215 Cytoplasmic. {ECO:0000255}.
TRANSMEM 216 236 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 237 259 Extracellular. {ECO:0000255}.
TRANSMEM 260 280 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 281 296 Cytoplasmic. {ECO:0000255}.
TRANSMEM 297 317 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 318 328 Extracellular. {ECO:0000255}.
TRANSMEM 329 349 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 350 358 Cytoplasmic. {ECO:0000255}.
TRANSMEM 359 378 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 379 383 Extracellular. {ECO:0000255}.
TRANSMEM 384 401 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 402 686 Cytoplasmic. {ECO:0000255}.
DOMAIN 258 398 Ferric oxidoreductase. {ECO:0000255}.
DOMAIN 399 522 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 462 468 FAD. {ECO:0000255}.
NP_BIND 514 517 NADP. {ECO:0000255}.
NP_BIND 652 653 NADP. {ECO:0000255}.
METAL 294 294 Iron (heme 1 axial ligand).
{ECO:0000269|PubMed:8940093}.
METAL 308 308 Iron (heme 2 axial ligand).
{ECO:0000269|PubMed:8940093}.
METAL 364 364 Iron (heme 1 axial ligand).
{ECO:0000269|PubMed:8940093}.
METAL 378 378 Iron (heme 2 axial ligand).
{ECO:0000269|PubMed:8940093}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 294 294 H->A: Impairs heme binding.
{ECO:0000269|PubMed:8940093}.
MUTAGEN 308 308 H->A: Impairs heme binding.
{ECO:0000269|PubMed:8940093}.
MUTAGEN 364 364 H->A: Impairs heme binding.
{ECO:0000269|PubMed:8940093}.
MUTAGEN 378 378 H->A: Impairs heme binding.
{ECO:0000269|PubMed:8940093}.
SEQUENCE 686 AA; 78854 MW; 7F6BB3B93A95D6A3 CRC64;
MVRTRVLFCL FISFFATVQS SATLISTSCI SQAALYQFGC SSKSKSCYCK NINWLGSVTA
CAYENSKSNK TLDSALMKLA SQCSSIKVYT LEDMKNIYLN ASNYLRAPEK SDKKTVVSQP
LMANETAYHY YYEENYGIHL NLMRSQWCAW GLVFFWVAVL TAATILNILK RVFGKNIMAN
SVKKSLIYPS VYKDYNERTF YLWKRLPFNF TTRGKGLVVL IFVILTILSL SFGHNIKLPH
PYDRPRWRRS MAFVSRRADL MAIALFPVVY LFGIRNNPFI PITGLSFSTF NFYHKWSAYV
CFMLAVVHSI VMTASGVKRG VFQSLVRKFY FRWGIVATIL MSIIIFQSEK VFRNRGYEIF
LLIHKAMNIM FIIAMYYHCH TLGWMGWIWS MAGILCFDRF CRIVRIIMNG GLKTATLSTT
DDSNVIKISV KKPKFFKYQV GAFAYMYFLS PKSAWFYSFQ SHPFTVLSER HRDPNNPDQL
TMYVKANKGI TRVLLSKVLS APNHTVDCKI FLEGPYGVTV PHIAKLKRNL VGVAAGLGVA
AIYPHFVECL RLPSTDQLQH KFYWIVNDLS HLKWFENELQ WLKEKSCEVS VIYTGSSVED
TNSDESTKGF DDKEESEITV ECLNKRPDLK ELVRSEIKLS ELENNNITFY SCGPATFNDD
FRNAVVQGID SSLKIDVELE EESFTW


Related products :

Catalog number Product name Quantity
EIAAB10258 CYBRD1,Cytochrome b reductase 1,DCYTB,Duodenal cytochrome b,Ferric-chelate reductase 3,FRRS3,Homo sapiens,Human
FRRS1_HUMAN Human ELISA Kit FOR Ferric-chelate reductase 1 96T
FRRS1_BOVIN Bovine ELISA Kit FOR Ferric-chelate reductase 1 96T
FRS3 FRRS1 Gene ferric-chelate reductase 1
E12435h Human Ferric Chelate Reductase 1 ELISA Kit 96T
FRRS1_MOUSE Mouse ELISA Kit FOR Ferric-chelate reductase 1 96T
CSB-EL009003HU Human Ferric-chelate reductase 1(FRRS1) ELISA kit 96T
CSB-EL009003BO Bovine Ferric-chelate reductase 1(FRRS1) ELISA kit 96T
CSB-EL009003MO Mouse Ferric-chelate reductase 1(FRRS1) ELISA kit 96T
CSB-EL009003BO Bovine Ferric-chelate reductase 1(FRRS1) ELISA kit SpeciesBovine 96T
CSB-EL009003MO Mouse Ferric-chelate reductase 1(FRRS1) ELISA kit SpeciesMouse 96T
CSB-EL009003HU Human Ferric-chelate reductase 1(FRRS1) ELISA kit SpeciesHuman 96T
FRRS1_MOUSE ELISA Kit FOR Ferric-chelate reductase 1; organism: Mouse; gene name: FRRS1 96T
CSB-EL009003MO Mouse ferric-chelate reductase 1 (FRRS1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL009003HU Human ferric-chelate reductase 1 (FRRS1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL009003BO Bovine ferric-chelate reductase 1 (FRRS1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
EIAAB13217 ANG1,Another new gene 1 protein,C-14 sterol reductase,Delta(14)-sterol reductase,Delta-14-SR,Homo sapiens,Human,Putative sterol reductase SR-1,Sterol C14-reductase,TM7SF2,Transmembrane 7 superfamily m
EIAAB13216 C-14 sterol reductase,C14SR,Delta(14)-sterol reductase,Delta-14-SR,Mouse,Mus musculus,Sterol C14-reductase,Tm7sf2,Transmembrane 7 superfamily member 2
EIAAB13218 Bos taurus,Bovine,C-14 sterol reductase,Delta(14)-sterol reductase,Delta-14-SR,Sterol C14-reductase,TM7SF2,Transmembrane 7 superfamily member 2
EIAAB10691 Carbonyl reductase II,DCXR,Dicarbonyl_L-xylulose reductase,Homo sapiens,Human,kiDCR,Kidney dicarbonyl reductase,L-xylulose reductase,Sperm surface protein P34H,XR
EIAAB11124 7-dehydrocholesterol reductase,7-DHC reductase,D7SR,DHCR7,Homo sapiens,Human,Putative sterol reductase SR-2,Sterol Delta(7)-reductase
E-03815/110 Ethylene Diamine Tetra Acetic Acid Ferric Sodium Salt (EDTA Ferric Sodium Salt) CAS: 1578-42-6 100 gm
E-03815/110 Ethylene Diamine Tetra Acetic Acid Ferric Sodium Salt (EDTA Ferric Sodium Salt) CAS: 1578-42-6 500 gm
EIAAB11126 7-dehydrocholesterol reductase,7-DHC reductase,Bos taurus,Bovine,DHCR7,Sterol Delta(7)-reductase
EIAAB11125 7-dehydrocholesterol reductase,7-DHC reductase,Dhcr7,Mouse,Mus musculus,Sterol Delta(7)-reductase


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
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