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

Neuroendocrine convertase 1 (NEC 1) (EC 3.4.21.93) (Furin homolog) (PC3) (Prohormone convertase 1) (Propeptide-processing protease) (Proprotein convertase 1) (PC1)

 NEC1_MOUSE              Reviewed;         753 AA.
P63239; P21662; P22546;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Neuroendocrine convertase 1;
Short=NEC 1;
EC=3.4.21.93;
AltName: Full=Furin homolog;
AltName: Full=PC3;
AltName: Full=Prohormone convertase 1;
AltName: Full=Propeptide-processing protease;
AltName: Full=Proprotein convertase 1;
Short=PC1;
Flags: Precursor;
Name=Pcsk1; Synonyms=Att-1, Nec-1, Nec1;
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].
TISSUE=Pituitary;
PubMed=1862107; DOI=10.1073/pnas.88.15.6834;
Korner J., Chun J., Harter D., Axel R.;
"Isolation and functional expression of a mammalian prohormone
processing enzyme, murine prohormone convertase 1.";
Proc. Natl. Acad. Sci. U.S.A. 88:6834-6838(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=LAF1;
PubMed=1657897;
Nakayama K., Hosaka M., Hatsuzawa K., Murakami K.;
"Cloning and functional expression of a novel endoprotease involved in
prohormone processing at dibasic sites.";
J. Biochem. 109:803-806(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Pituitary;
PubMed=2017186; DOI=10.1210/mend-5-1-111;
Seidah N.G., Marcinkiewicz M., Benjannet S., Gaspar L., Beaubien G.,
Mattei M.-G., Lazure C., Mbikay M., Chretien M.;
"Cloning and primary sequence of a mouse candidate prohormone
convertase PC1 homologous to PC2, Furin, and Kex2: distinct
chromosomal localization and messenger RNA distribution in brain and
pituitary compared to PC2.";
Mol. Endocrinol. 5:111-122(1991).
[4]
PROTEIN SEQUENCE OF 111-120.
TISSUE=Ovary;
PubMed=8449925;
Zhou Y., Lindberg I.;
"Purification and characterization of the prohormone convertase
PC1(PC3).";
J. Biol. Chem. 268:5615-5623(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 214-478.
TISSUE=Pituitary;
PubMed=2169760; DOI=10.1089/dna.1990.9.415;
Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
Chretien M.;
"cDNA sequence of two distinct pituitary proteins homologous to Kex2
and furin gene products: tissue-specific mRNAs encoding candidates for
pro-hormone processing proteinases.";
DNA Cell Biol. 9:415-424(1990).
[6]
ERRATUM.
PubMed=2264933; DOI=10.1089/dna.1990.9.789;
Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
Chretien M.;
DNA Cell Biol. 9:789-789(1990).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16384863; DOI=10.1210/en.2005-1373;
Creemers J.W., Pritchard L.E., Gyte A., Le Rouzic P., Meulemans S.,
Wardlaw S.L., Zhu X., Steiner D.F., Davies N., Armstrong D.,
Lawrence C.B., Luckman S.M., Schmitz C.A., Davies R.A., Brennand J.C.,
White A.;
"Agouti-related protein is posttranslationally cleaved by proprotein
convertase 1 to generate agouti-related protein (AGRP)83-132:
interaction between AGRP83-132 and melanocortin receptors cannot be
influenced by syndecan-3.";
Endocrinology 147:1621-1631(2006).
[8]
STRUCTURE BY NMR OF 28-110.
PubMed=12095256; DOI=10.1016/S0022-2836(02)00543-0;
Tangrea M.A., Bryan P.N., Sari N., Orban J.;
"Solution structure of the pro-hormone convertase 1 pro-domain from
Mus musculus.";
J. Mol. Biol. 320:801-812(2002).
-!- FUNCTION: Involved in the processing of hormone and other protein
precursors at sites comprised of pairs of basic amino acid
residues. Substrates include POMC, renin, enkephalin, dynorphin,
somatostatin, insulin and AGRP. {ECO:0000269|PubMed:16384863}.
-!- CATALYTIC ACTIVITY: Release of protein hormones, neuropeptides and
renin from their precursors, generally by hydrolysis of -Lys-
Arg-|- bonds.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5-6.5.;
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15770815, EBI-15770815;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
Note=Localized in the secretion granules.
-!- DISRUPTION PHENOTYPE: Increase in unprocessed AGRP.
{ECO:0000269|PubMed:16384863}.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M69196; AAA39732.1; -; mRNA.
EMBL; X57088; CAA40368.1; -; mRNA.
EMBL; M58589; AAA39894.1; -; mRNA.
EMBL; M55668; AAA39375.1; ALT_SEQ; mRNA.
CCDS; CCDS26649.1; -.
PIR; JX0171; KXMSC1.
RefSeq; NP_038656.1; NM_013628.2.
RefSeq; XP_006517216.1; XM_006517153.2.
RefSeq; XP_006517217.1; XM_006517154.3.
RefSeq; XP_006517218.1; XM_006517155.2.
UniGene; Mm.1333; -.
UniGene; Mm.394672; -.
PDB; 1KN6; NMR; -; A=28-110.
PDB; 2KDT; NMR; -; A=711-753.
PDB; 2KE3; NMR; -; A=711-753.
PDBsum; 1KN6; -.
PDBsum; 2KDT; -.
PDBsum; 2KE3; -.
ProteinModelPortal; P63239; -.
SMR; P63239; -.
DIP; DIP-48841N; -.
STRING; 10090.ENSMUSP00000022075; -.
MEROPS; S08.072; -.
iPTMnet; P63239; -.
PhosphoSitePlus; P63239; -.
PaxDb; P63239; -.
PeptideAtlas; P63239; -.
PRIDE; P63239; -.
Ensembl; ENSMUST00000022075; ENSMUSP00000022075; ENSMUSG00000021587.
GeneID; 18548; -.
KEGG; mmu:18548; -.
UCSC; uc007rfs.1; mouse.
CTD; 5122; -.
MGI; MGI:97511; Pcsk1.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; P63239; -.
KO; K01359; -.
OMA; FEPRALK; -.
OrthoDB; EOG091G05HI; -.
PhylomeDB; P63239; -.
TreeFam; TF314277; -.
BRENDA; 3.4.21.93; 3474.
Reactome; R-MMU-167060; NGF processing.
Reactome; R-MMU-209952; Peptide hormone biosynthesis.
Reactome; R-MMU-264876; Insulin processing.
Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-MMU-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
EvolutionaryTrace; P63239; -.
PMAP-CutDB; P63239; -.
PRO; PR:P63239; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021587; -.
CleanEx; MM_PCSK1; -.
ExpressionAtlas; P63239; baseline and differential.
Genevisible; P63239; MM.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0032455; P:nerve growth factor processing; TAS:Reactome.
GO; GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR022005; Proho_convert.
InterPro; IPR002884; PrprotnconvertsP.
InterPro; IPR032815; S8_pro-domain.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF12177; Proho_convert; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cleavage on pair of basic residues;
Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
Serine protease; Signal; Zymogen.
SIGNAL 1 27 {ECO:0000255}.
PROPEP 28 110 {ECO:0000255}.
/FTId=PRO_0000027059.
CHAIN 111 753 Neuroendocrine convertase 1.
/FTId=PRO_0000027060.
DOMAIN 162 451 Peptidase S8.
DOMAIN 460 597 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
ACT_SITE 167 167 Charge relay system. {ECO:0000250}.
ACT_SITE 208 208 Charge relay system. {ECO:0000250}.
ACT_SITE 382 382 Charge relay system. {ECO:0000250}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 645 645 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 225 374 {ECO:0000250}.
DISULFID 317 347 {ECO:0000250}.
DISULFID 467 494 {ECO:0000250}.
CONFLICT 112 112 V -> F (in Ref. 2; CAA40368).
{ECO:0000305}.
CONFLICT 117 117 A -> P (in Ref. 2; CAA40368).
{ECO:0000305}.
CONFLICT 122 122 N -> T (in Ref. 2; CAA40368).
{ECO:0000305}.
CONFLICT 128 128 Q -> H (in Ref. 2; CAA40368).
{ECO:0000305}.
CONFLICT 282 282 R -> K (in Ref. 2; CAA40368).
{ECO:0000305}.
CONFLICT 330 330 S -> L (in Ref. 3; AAA39375).
{ECO:0000305}.
CONFLICT 732 732 K -> E (in Ref. 2; CAA40368).
{ECO:0000305}.
STRAND 35 38 {ECO:0000244|PDB:1KN6}.
HELIX 43 53 {ECO:0000244|PDB:1KN6}.
STRAND 62 65 {ECO:0000244|PDB:1KN6}.
STRAND 67 71 {ECO:0000244|PDB:1KN6}.
STRAND 77 79 {ECO:0000244|PDB:1KN6}.
HELIX 89 94 {ECO:0000244|PDB:1KN6}.
STRAND 97 100 {ECO:0000244|PDB:1KN6}.
STRAND 713 716 {ECO:0000244|PDB:2KDT}.
STRAND 718 721 {ECO:0000244|PDB:2KE3}.
HELIX 722 726 {ECO:0000244|PDB:2KDT}.
TURN 727 730 {ECO:0000244|PDB:2KDT}.
HELIX 741 748 {ECO:0000244|PDB:2KDT}.
TURN 749 751 {ECO:0000244|PDB:2KDT}.
SEQUENCE 753 AA; 84174 MW; 04239C7B6385382E CRC64;
MEQRGWTLQC TAFAFFCVWC ALNSVKAKRQ FVNEWAAEIP GGQEAASAIA EELGYDLLGQ
IGSLENHYLF KHKSHPRRSR RSALHITKRL SDDDRVTWAE QQYEKERSKR SVQKDSALDL
FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWEKGITGKG VVITVLDDGL EWNHTDIYAN
YDPEASYDFN DNDHDPFPRY DLTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM
LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
ASNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECVVK DNNFEPRALK
ANGEVIVEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAVG TSTVLLAERE
RDTSPNGFKN WDFMSVHTWG ENPVGTWTLK ITDMSGRMQN EGRIVNWKLI LHGTSSQPEH
MKQPRVYTSY NTVQNDRRGV EKMVNVVEKR PTQKSLNGNL LVPKNSSSSN VEGRRDEQVQ
GTPSKAMLRL LQSAFSKNAL SKQSPKKSPS AKLSIPYESF YEALEKLNKP SKLEGSEDSL
YSDYVDVFYN TKPYKHRDDR LLQALMDILN EEN


Related products :

Catalog number Product name Quantity
EIAAB26834 Att-1,Furin homolog,Mouse,Mus musculus,NEC 1,Nec1,Nec-1,Neuroendocrine convertase 1,PC1,PC3,Pcsk1,Prohormone convertase 1,Propeptide-processing protease,Proprotein convertase 1
EIAAB30210 Homo sapiens,hPC8,Human,LPC,Lymphoma proprotein convertase,PC7,PC7,PC8,PC8,PCSK7,Prohormone convertase 7,Proprotein convertase 7,Proprotein convertase 8,Proprotein convertase subtilisin_kexin type 7,S
EIAAB26832 Homo sapiens,Human,NEC 1,NEC1,Neuroendocrine convertase 1,PC1,PCSK1,Prohormone convertase 1,Proprotein convertase 1
EIAAB26831 Bdp,NEC 1,Nec1,Nec-1,Neuroendocrine convertase 1,PC1,Pcsk1,Prohormone convertase 1,Proprotein convertase 1,Rat,Rattus norvegicus
EIAAB26839 KEX2-like endoprotease 2,NEC 2,Neuroendocrine convertase 2,PC2,PC2,PCSK2,Pig,Prohormone convertase 2,Proprotein convertase 2,Sus scrofa
EIAAB26838 KEX2-like endoprotease 2,Mouse,Mus musculus,NEC 2,Nec2,Nec-2,Neuroendocrine convertase 2,PC2,Pcsk2,Prohormone convertase 2,Proprotein convertase 2
EIAAB26833 Bos taurus,Bovine,NEC 1,Neuroendocrine convertase 1,PC1,PCSK1,Prohormone convertase 1,Proprotein convertase 1
EIAAB26835 Bos taurus,Bovine,NEC 2,Neuroendocrine convertase 2,PC2,PCSK2,Prohormone convertase 2,Proprotein convertase 2
EIAAB26836 KEX2-like endoprotease 2,NEC 2,Nec2,Nec-2,Neuroendocrine convertase 2,PC2,Pcsk2,Prohormone convertase 2,Proprotein convertase 2,Rat,Rattus norvegicus,Rpc2
EIAAB26837 Homo sapiens,Human,KEX2-like endoprotease 2,NEC 2,NEC2,Neuroendocrine convertase 2,PC2,PCSK2,Prohormone convertase 2,Proprotein convertase 2
EIAAB30201 KEX2-like endoprotease 3,Mouse,Mus musculus,NEC 3,Nec3,Nec-3,Neuroendocrine convertase 3,Pcsk4,Prohormone convertase 3,Proprotein convertase subtilisin_kexin type 4
EIAAB30202 KEX2-like endoprotease 3,NEC 3,Nec3,Nec-3,Neuroendocrine convertase 3,PC4,Pcsk4,Prohormone convertase 3,Proprotein convertase subtilisin_kexin type 4,Rat,Rattus norvegicus
EIAAB30209 Mouse,Mus musculus,PC7,Pc7,Pcsk7,Prohormone convertase 7,Proprotein convertase 7,Proprotein convertase subtilisin_kexin type 7,SPC7,Subtilisin_kexin-like protease PC7,Subtilisin-like proprotein conver
EIAAB30211 PC7,Pc7,Pcsk7,Prohormone convertase 7,Proprotein convertase 7,Proprotein convertase subtilisin_kexin type 7,Rat,Rattus norvegicus,rPC7,Subtilisin_kexin-like protease PC7
EIAAB30205 Mouse,Mus musculus,PC5,PC6,Pcsk5,Proprotein convertase 5,Proprotein convertase 6,Proprotein convertase subtilisin_kexin type 5,SPC6,Subtilisin_kexin-like protease PC5,Subtilisin-like proprotein conver
EIAAB30204 Homo sapiens,hPC6,Human,PC5,PC5,PC6,PC6,PCSK5,Proprotein convertase 5,Proprotein convertase 6,Proprotein convertase subtilisin_kexin type 5,Subtilisin_kexin-like protease PC5
EIAAB30212 Narc1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,Pcsk9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,Rat,Rattus norvegicus,Subtilisin_kexin-like protease PC9
EIAAB30213 Mouse,Mus musculus,Narc1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,Pcsk9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,Subtilisin_kexin-like protease PC9
EIAAB30214 Homo sapiens,Human,NARC1,NARC-1,Neural apoptosis-regulated convertase 1,PC9,PCSK9,Proprotein convertase 9,Proprotein convertase subtilisin_kexin type 9,PSEC0052,Subtilisin_kexin-like protease PC9
EIAAB30206 PC5,PC6,Pcsk5,Proprotein convertase 5,Proprotein convertase 6,Proprotein convertase subtilisin_kexin type 5,Rat,Rattus norvegicus,rPC5,Subtilisin_kexin-like protease PC5
Y051640 Anti-PC9 (paired basic amino acid cleaving enzyme-9, PCSK9, proprotein convertase subtilisin_kexin type 9a, NARC-1, neural apoptosis regulated convertase 1); Propeptide domain Antibody 100μg
Y051640 Anti-PC9 paired basic amino acid cleaving enzyme-9 PCSK9 proprotein convertase subtilisin per kexin type 9a NARC-1 neural apoptosis regulated convertase 1; Propeptide domain antibody 250ug
EIAAB30207 Homo sapiens,Human,PACE4,Paired basic amino acid cleaving enzyme 4,PCSK6,Proprotein convertase subtilisin_kexin type 6,SPC4,Subtilisin_kexin-like protease PACE4,Subtilisin-like proprotein convertase 4
EIAAB30203 Homo sapiens,Human,PC4,PC4,PCSK4,Proprotein convertase 4,Proprotein convertase subtilisin_kexin type 4,UNQ2757_PRO6496
18-272-195521 NEC2 - Rabbit polyclonal to NEC2; EC 3.4.21.94; NEC 2; PC2; Prohormone convertase 2; Proprotein convertase 2; KEX2-like endoprotease 2 Polyclonal 0.05 ml


 

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