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

Angiotensin-converting enzyme (ACE) (EC 3.2.1.-) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) (CD antigen CD143) [Cleaved into: Angiotensin-converting enzyme, soluble form]

 ACE_RABIT               Reviewed;        1310 AA.
P12822; O02852; P22968;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
25-OCT-2017, entry version 135.
RecName: Full=Angiotensin-converting enzyme;
Short=ACE;
EC=3.2.1.-;
EC=3.4.15.1;
AltName: Full=Dipeptidyl carboxypeptidase I;
AltName: Full=Kininase II;
AltName: CD_antigen=CD143;
Contains:
RecName: Full=Angiotensin-converting enzyme, soluble form;
Flags: Precursor;
Name=ACE; Synonyms=DCP1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
TISSUE=Lung;
PubMed=1311831; DOI=10.1093/nar/20.4.683;
Thekkumkara T.J., Livingston W. III, Kumar R.S., Sen G.C.;
"Use of alternative polyadenylation sites for tissue-specific
transcription of two angiotensin-converting enzyme mRNAs.";
Nucleic Acids Res. 20:683-687(1992).
[2]
SEQUENCE REVISION.
Sen G.C.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
STRAIN=New Zealand white; TISSUE=Testis;
PubMed=2550457;
Kumar R.S., Kusari J., Roy S.N., Soffer R.L., Sen G.C.;
"Structure of testicular angiotensin-converting enzyme. A segmental
mosaic isozyme.";
J. Biol. Chem. 264:16754-16758(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88, AND ALTERNATIVE SPLICING.
TISSUE=Liver;
PubMed=1847388;
Kumar R.S., Thekkumkara T.J., Sen G.C.;
"The mRNAs encoding the two angiotensin-converting isozymes are
transcribed from the same gene by a tissue-specific choice of
alternative transcription initiation sites.";
J. Biol. Chem. 266:3854-3862(1991).
[5]
PROTEIN SEQUENCE OF 34-44 AND 755-758.
PubMed=6291514; DOI=10.1016/0006-291X(82)90634-9;
Iwata K., Lai C.Y., El-Dorry H.A., Soffer R.L.;
"The NH2- and COOH-terminal sequences of the angiotensin-converting
enzyme isozymes from rabbit lung and testis.";
Biochem. Biophys. Res. Commun. 107:1097-1103(1982).
[6]
PROTEIN SEQUENCE OF 34-55.
TISSUE=Lung;
PubMed=6314908; DOI=10.1016/0003-9861(83)90362-4;
Iwata K., Blacher R., Soffer R.L., Lai C.Y.;
"Rabbit pulmonary angiotensin-converting enzyme: the NH2-terminal
fragment with enzymatic activity and its formation from the native
enzyme by NH4OH treatment.";
Arch. Biochem. Biophys. 227:188-201(1983).
[7]
PROTEIN SEQUENCE OF 34-55, AND GLYCOSYLATION.
PubMed=1654880; DOI=10.1042/bj2780375;
Kirley T.L.;
"The Mg(2+)-ATPase of rabbit skeletal-muscle transverse tubule is a
highly glycosylated multiple-subunit enzyme.";
Biochem. J. 278:375-380(1991).
[8]
NUCLEOTIDE SEQUENCE OF 646-746.
PubMed=1705622;
Sen G.C., Thekkumkara T.J., Kumar R.S.;
"Angiotensin-converting enzyme: structural relationship of the
testicular and the pulmonary forms.";
J. Cardiovasc. Pharmacol. 16:S14-S18(1990).
[9]
PROTEIN SEQUENCE OF 727-733 AND 809-815.
PubMed=2176870; DOI=10.1021/bi00498a011;
Chen Y.N., Riordan J.F.;
"Identification of essential tyrosine and lysine residues in
angiotensin converting enzyme: evidence for a single active site.";
Biochemistry 29:10493-10498(1990).
[10]
PROTEIN SEQUENCE OF 1237-1259, AND CLEAVAGE SITE.
PubMed=8294466;
Ramchandran R., Sen G.C., Misono K., Sen I.;
"Regulated cleavage-secretion of the membrane-bound angiotensin-
converting enzyme.";
J. Biol. Chem. 269:2125-2130(1994).
[11]
MUTAGENESIS OF LYS-727 AND TYR-809, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7902354;
Sen I., Kasturi S., Abdul-Jabbar M., Sen G.C.;
"Mutations in two specific residues of testicular angiotensin-
converting enzyme change its catalytic properties.";
J. Biol. Chem. 268:25748-25754(1993).
-!- FUNCTION: Converts angiotensin I to angiotensin II by release of
the terminal His-Leu, this results in an increase of the
vasoconstrictor activity of angiotensin. Also able to inactivate
bradykinin, a potent vasodilator. Has also a glycosidase activity
which releases GPI-anchored proteins from the membrane by cleaving
the mannose linkage in the GPI moiety (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither
Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II,
with increase in vasoconstrictor activity, but no action on
angiotensin II.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. Isoform Testis-specific only
binds 1 Zn(2+) ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
Note=Binds 3 chloride ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Strongly activated by chloride. Specifically
inhibited by lisinopril. {ECO:0000269|PubMed:7902354}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.6 mM for Hip-His-Leu {ECO:0000269|PubMed:7902354};
KM=0.09 mM for angiotensin I {ECO:0000269|PubMed:7902354};
-!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
Secreted {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
Note=Detected in both cell membrane and cytoplasm in neurons.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Somatic;
IsoId=P12822-1; Sequence=Displayed;
Name=Testis-specific; Synonyms=ACE-T;
IsoId=P12822-2, P22968-1;
Sequence=VSP_037644, VSP_037645;
-!- TISSUE SPECIFICITY: Testis-specific isoform is expressed in
spermatocytes, adult testis.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:1654880}.
-!- PTM: Phosphorylated by CK2 on Ser-1303; which allows membrane
retention. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X62551; CAA44428.1; -; mRNA.
EMBL; J05041; AAA31153.1; -; mRNA.
EMBL; M58579; AAA31151.1; ALT_SEQ; Genomic_DNA.
EMBL; M58580; AAA31152.1; -; Genomic_DNA.
PIR; A34402; A34402.
PIR; S35484; S35484.
RefSeq; NP_001075864.1; NM_001082395.1. [P12822-1]
RefSeq; NP_001164540.1; NM_001171069.1. [P12822-2]
UniGene; Ocu.1824; -.
ProteinModelPortal; P12822; -.
SMR; P12822; -.
STRING; 9986.ENSOCUP00000016378; -.
BindingDB; P12822; -.
ChEMBL; CHEMBL4074; -.
MEROPS; M02.001; -.
PRIDE; P12822; -.
GeneID; 100009274; -.
KEGG; ocu:100009274; -.
CTD; 1636; -.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
HOGENOM; HOG000007838; -.
HOVERGEN; HBG000264; -.
InParanoid; P12822; -.
KO; K01283; -.
SABIO-RK; P12822; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
CDD; cd06461; M2_ACE; 2.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 2.
Pfam; PF01401; Peptidase_M2; 2.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 2.
1: Evidence at protein level;
Alternative splicing; Carboxypeptidase; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 33 {ECO:0000269|PubMed:1654880,
ECO:0000269|PubMed:6291514,
ECO:0000269|PubMed:6314908}.
CHAIN 34 1310 Angiotensin-converting enzyme.
/FTId=PRO_0000028551.
CHAIN 34 1236 Angiotensin-converting enzyme, soluble
form.
/FTId=PRO_0000028552.
PROPEP 1237 1310 Removed in secreted form. {ECO:0000250}.
/FTId=PRO_0000028553.
TOPO_DOM 34 1260 Extracellular. {ECO:0000255}.
TRANSMEM 1261 1281 Helical. {ECO:0000255}.
TOPO_DOM 1282 1310 Cytoplasmic. {ECO:0000255}.
REGION 35 634 Peptidase M2 1.
REGION 635 1236 Peptidase M2 2.
ACT_SITE 396 396 1. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
ACT_SITE 993 993 2. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 395 395 Zinc 1; catalytic. {ECO:0000250}.
METAL 399 399 Zinc 1; catalytic. {ECO:0000250}.
METAL 422 422 Zinc 1; catalytic. {ECO:0000250}.
METAL 992 992 Zinc 2; catalytic. {ECO:0000250}.
METAL 996 996 Zinc 2; catalytic. {ECO:0000250}.
METAL 1020 1020 Zinc 2; catalytic. {ECO:0000250}.
BINDING 236 236 Chloride 1. {ECO:0000250}.
BINDING 533 533 Chloride 1. {ECO:0000250}.
BINDING 795 795 Chloride 2. {ECO:0000250}.
BINDING 833 833 Chloride 3. {ECO:0000250}.
BINDING 1094 1094 Chloride 2. {ECO:0000250}.
BINDING 1098 1098 Chloride 2. {ECO:0000250}.
BINDING 1131 1131 Chloride 3. {ECO:0000250}.
SITE 1237 1238 Cleavage.
MOD_RES 1303 1303 Phosphoserine.
{ECO:0000250|UniProtKB:P12821}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 681 681 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 718 718 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 946 946 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1195 1195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 162 170 {ECO:0000250}.
DISULFID 761 767 {ECO:0000250}.
DISULFID 961 979 {ECO:0000250}.
DISULFID 1147 1159 {ECO:0000250}.
VAR_SEQ 1 573 Missing (in isoform Testis-specific).
{ECO:0000303|PubMed:2550457}.
/FTId=VSP_037644.
VAR_SEQ 574 645 RAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWL
QEQNERNGEVLGWPEYQWRPPLPNNYPEGID -> MGQGWA
APGLPSLLLLLLCCGHSLLVPSRVAARRVTVNQGTTSQATT
TSKATTSIRATTHQTTAHQTTQSPN (in isoform
Testis-specific).
{ECO:0000303|PubMed:2550457}.
/FTId=VSP_037645.
MUTAGEN 727 727 K->E: No effect on activity. 20-fold
reduction in catalytic efficiency; when
associated with F-809.
{ECO:0000269|PubMed:7902354}.
MUTAGEN 809 809 Y->F: No effect on activity. 20-fold
reduction in catalytic efficiency; when
associated with E-727.
{ECO:0000269|PubMed:7902354}.
CONFLICT 48 48 E -> N (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 1310 AA; 150406 MW; 04777FAB17981DEA CRC64;
MGAAPGRRGP RLLRPPPPLL LLLLLLRPPP AALTLDPGLL PGDFAADEAG ARLFASSYNS
SAEQVLFRST AASWAHDTNI TAENARRQEE EALLSQEFAE AWGKKAKELY DPVWQNFTDP
ELRRIIGAVR TLGPANLPLA KRQQYNSLLS NMSQIYSTGK VCFPNKTASC WSLDPDLNNI
LASSRSYAML LFAWEGWHNA VGIPLKPLYQ EFTALSNEAY RQDGFSDTGA YWRSWYDSPT
FEEDLERIYH QLEPLYLNLH AYVRRVLHRR YGDRYINLRG PIPAHLLGNM WAQSWESIYD
MVVPFPDKPN LDVTSTMVQK GWNATHMFRV AEEFFTSLGL LPMPPEFWAE SMLEKPEDGR
EVVCHASAWD FYNRKDFRIK QCTQVTMDQL STVHHEMGHV QYYLQYKDQP VSLRRANPGF
HEAIGDVLAL SVSTPAHLHK IGLLDHVTND TESDINYLLK MALEKIAFLP FGYLVDQWRW
GVFSGRTPSS RYNFDWWYLR TKYQGICPPV VRNETHFDAG AKFHIPSVTP YIRYFVSFVL
QFQFHQALCM EAGHQGPLHQ CDIYQSTRAG AKLRAVLQAG CSRPWQEVLK DMVASDALDA
QPLLDYFQPV TQWLQEQNER NGEVLGWPEY QWRPPLPNNY PEGIDLVTDE AEASRFVEEY
DRSFQAVWNE YAEANWNYNT NITTEASKIL LQKNMQIANH TLTYGNWARR FDVSNFQNAT
SKRIIKKVQD LQRAVLPVKE LEEYNQILLD METIYSVANV CRVDGSCLQL EPDLTNLMAT
SRKYDELLWV WTSWRDKVGR AILPYFPKYV EFTNKAARLN GYVDAGDSWR SMYETPTLEQ
DLERLFQELQ PLYLNLHAYV GRALHRHYGA QHINLEGPIP AHLLGNMWAQ TWSNIYDLVA
PFPSASTMDA TEAMIKQGWT PRRMFEEADK FFISLGLLPV PPEFWNKSML EKPTDGREVV
CHASAWDFYN GKDFRIKQCT TVNMEDLVVV HHEMGHIQYF MQYKDLPVAL REGANPGFHE
AIGDVLALSV STPKHLHSIN LLSSEGGGYE HDINFLMKMA LDKIAFIPFS YLVDEWRWRV
FDGSITKENY NQEWWSLRLK YQGLCPPAPR SQGDFDPGAK FHIPSSVPYI RYFVSFIIQF
QFHEALCKAA GHTGPLHTCD IYQSKEAGKR LADAMKLGYS KPWPEAMKVI TGQPNMSASA
MMNYFKPLMD WLLTENGRHG EKLGWPQYTW TPNSARSEGS LPDSGRVNFL GMNLDAQQAR
VGQWVLLFLG VALLLASLGL TQRLFSIRYQ SLRQPHHGPQ FGSEVELRHS


Related products :

Catalog number Product name Quantity
20-272-190613 Angiotensin Converting Enzyme - Mouse monoclonal [ 9B9] to Angiotensin Converting Enzyme; EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.5 ml
20-272-190612 Angiotensin Converting Enzyme - Mouse monoclonal [3C5] to Angiotensin Converting Enzyme; EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.5 ml
20-272-190609 Angiotensin Converting Enzyme - Mouse monoclonal [2E2] to Angiotensin Converting Enzyme; EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.5 ml
20-272-190598 Angiotensin Converting Enzyme ( FITC ) - Mouse monoclonal [ i1A8] to Angiotensin Converting Enzyme ( FITC ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
20-272-190610 Angiotensin Converting Enzyme ( Biotin ) - Mouse monoclonal [i2H5] to Angiotensin Converting Enzyme ( Biotin ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
20-272-190611 Angiotensin Converting Enzyme ( FITC ) - Mouse monoclonal [i2H5] to Angiotensin Converting Enzyme ( FITC ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
20-272-190614 Angiotensin Converting Enzyme ( Biotin ) - Mouse monoclonal [9B9] to Angiotensin Converting Enzyme ( Biotin ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
20-272-190615 Angiotensin Converting Enzyme ( FITC ) - Mouse monoclonal [9B9] to Angiotensin Converting Enzyme ( FITC ); EC 3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143 antigen Monoclonal 0.05 mg
E0004m ELISA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
U0004b CLIA ACE,ACE,Angiotensin-converting enzyme,Bos taurus,Bovine,DCP1,Dipeptidyl carboxypeptidase I,Kininase II 96T
E0004r ELISA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Rat,Rattus norvegicus 96T
E0004b ELISA ACE,ACE,Angiotensin-converting enzyme,Bos taurus,Bovine,DCP1,Dipeptidyl carboxypeptidase I,Kininase II 96T
U0004r CLIA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Rat,Rattus norvegicus 96T
E0004r ELISA kit ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Rat,Rattus norvegicus 96T
E0004m ELISA kit ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
E0004b ELISA kit ACE,ACE,Angiotensin-converting enzyme,Bos taurus,Bovine,DCP1,Dipeptidyl carboxypeptidase I,Kininase II 96T
U0004m CLIA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
E0004h ELISA kit ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
U0004h CLIA ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
E0004Rb ELISA kit ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
E0004Rb ELISA ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
U0004Rb CLIA ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
E0004h ELISA ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
U1886h CLIA kit ACE2,ACEH,ACE-related carboxypeptidase,Angiotensin-converting enzyme 2,Angiotensin-converting enzyme homolog,Homo sapiens,Human,Metalloprotease MPROT15,UNQ868_PRO1885 96T
E1886h ELISA kit ACE2,ACEH,ACE-related carboxypeptidase,Angiotensin-converting enzyme 2,Angiotensin-converting enzyme homolog,Homo sapiens,Human,Metalloprotease MPROT15,UNQ868_PRO1885 96T


 

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