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

Transmembrane protease serine 13 (EC 3.4.21.-) (Membrane-type mosaic serine protease) (Mosaic serine protease)

 TMPSD_HUMAN             Reviewed;         586 AA.
Q9BYE2; B4DTM9; E9PIJ5; F8WAJ3; Q86YM4; Q96JY8; Q9BYE1;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 4.
12-SEP-2018, entry version 133.
RecName: Full=Transmembrane protease serine 13;
EC=3.4.21.-;
AltName: Full=Membrane-type mosaic serine protease;
Short=Mosaic serine protease;
Name=TMPRSS13; Synonyms=MSP, TMPRSS11;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), POLYMORPHISM, AND
TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=11267681; DOI=10.1016/S0167-4781(01)00184-1;
Kim D.R., Sharmin S., Inoue M., Kido H.;
"Cloning and expression of novel mosaic serine proteases with and
without a transmembrane domain from human lung.";
Biochim. Biophys. Acta 1518:204-209(2001).
[2]
SEQUENCE REVISION TO 192; 259; 298 AND 496.
Kim D.R., Inoue M., Kido H.;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Park T.J., Park W.J.;
"Homo sapiens transmembrane protease, serine 6 (TMPRSS6) mRNA.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=MSPL, Large form, Membrane-type;
IsoId=Q9BYE2-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYE2-2; Sequence=VSP_013103, VSP_013104;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9BYE2-5; Sequence=VSP_013099;
Name=3; Synonyms=MSPS, Small form;
IsoId=Q9BYE2-3; Sequence=VSP_013099, VSP_013102;
Name=4;
IsoId=Q9BYE2-4; Sequence=VSP_013100, VSP_013101;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are predominantly
expressed in lung, placenta, pancreas, and prostate. Isoform 3 is
weakly expressed in testis and peripheral blood lymphocytes.
{ECO:0000269|PubMed:11267681}.
-!- POLYMORPHISM: The repeat A-S-P-A-[GLQR] is polymorphic and the
number of copies varies between 12 to 14.
{ECO:0000269|PubMed:11267681}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: Was termed TMPRSS6 (Ref.3). {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; AB048796; BAB39741.2; -; mRNA.
EMBL; AB048797; BAB39742.2; -; mRNA.
EMBL; AY190317; AAO38062.1; -; mRNA.
EMBL; AK027798; BAB55376.1; -; mRNA.
EMBL; AK300283; BAG62041.1; -; mRNA.
EMBL; AP002962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS55788.1; -. [Q9BYE2-3]
CCDS; CCDS55789.1; -. [Q9BYE2-4]
CCDS; CCDS58185.1; -. [Q9BYE2-2]
RefSeq; NP_001193718.1; NM_001206789.1. [Q9BYE2-3]
RefSeq; NP_001193719.1; NM_001206790.1. [Q9BYE2-4]
RefSeq; NP_001231924.1; NM_001244995.1. [Q9BYE2-2]
UniGene; Hs.266308; -.
ProteinModelPortal; Q9BYE2; -.
SMR; Q9BYE2; -.
BioGrid; 123845; 4.
STRING; 9606.ENSP00000434279; -.
MEROPS; S01.087; -.
iPTMnet; Q9BYE2; -.
PhosphoSitePlus; Q9BYE2; -.
BioMuta; TMPRSS13; -.
DMDM; 313104278; -.
PaxDb; Q9BYE2; -.
PeptideAtlas; Q9BYE2; -.
PRIDE; Q9BYE2; -.
ProteomicsDB; 79624; -.
ProteomicsDB; 79625; -. [Q9BYE2-2]
ProteomicsDB; 79626; -. [Q9BYE2-3]
ProteomicsDB; 79627; -. [Q9BYE2-4]
ProteomicsDB; 79628; -. [Q9BYE2-5]
Ensembl; ENST00000430170; ENSP00000387702; ENSG00000137747. [Q9BYE2-2]
Ensembl; ENST00000526090; ENSP00000436502; ENSG00000137747. [Q9BYE2-4]
Ensembl; ENST00000528626; ENSP00000435813; ENSG00000137747. [Q9BYE2-3]
GeneID; 84000; -.
KEGG; hsa:84000; -.
UCSC; uc001pru.3; human. [Q9BYE2-1]
CTD; 84000; -.
DisGeNET; 84000; -.
EuPathDB; HostDB:ENSG00000137747.14; -.
GeneCards; TMPRSS13; -.
HGNC; HGNC:29808; TMPRSS13.
MIM; 610050; gene.
neXtProt; NX_Q9BYE2; -.
OpenTargets; ENSG00000137747; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118962; -.
HOGENOM; HOG000251822; -.
HOVERGEN; HBG013304; -.
InParanoid; Q9BYE2; -.
KO; K09643; -.
GenomeRNAi; 84000; -.
PRO; PR:Q9BYE2; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137747; Expressed in 98 organ(s), highest expression level in skin of leg.
CleanEx; HS_TMPRSS13; -.
ExpressionAtlas; Q9BYE2; baseline and differential.
Genevisible; Q9BYE2; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
CDD; cd00112; LDLa; 1.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 3.10.250.10; -; 1.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR017327; Peptidase_S1A_TMPRSS13.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF15494; SRCR_2; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF037935; TMPRSS13; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00202; SR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF56487; SSF56487; 1.
PROSITE; PS50287; SRCR_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Membrane; Polymorphism; Protease; Reference proteome;
Repeat; Serine protease; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 586 Transmembrane protease serine 13.
/FTId=PRO_0000088698.
TOPO_DOM 1 165 Cytoplasmic. {ECO:0000255}.
TRANSMEM 166 186 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 187 586 Extracellular. {ECO:0000255}.
REPEAT 9 13 1-1.
REPEAT 14 18 2-1; approximate.
REPEAT 19 23 1-2.
REPEAT 24 28 1-3.
REPEAT 29 33 2-2.
REPEAT 34 38 1-4.
REPEAT 39 43 1-5.
REPEAT 44 48 1-6.
REPEAT 49 53 2-3.
REPEAT 54 58 1-7.
REPEAT 59 63 1-8.
REPEAT 64 68 2-4.
REPEAT 69 78 1-9; approximate.
REPEAT 79 83 1-10.
REPEAT 84 88 1-11.
REPEAT 89 93 1-12.
DOMAIN 195 325 SRCR. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 204 226 LDL-receptor class A.
DOMAIN 326 559 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 9 93 13 X 5 AA repeats of A-S-P-A-[GLQR].
REGION 14 68 4 X 5 AA repeats of T-P-P-G-R.
COMPBIAS 9 94 Ala-rich.
ACT_SITE 366 366 Charge relay system. {ECO:0000250}.
ACT_SITE 414 414 Charge relay system. {ECO:0000250}.
ACT_SITE 511 511 Charge relay system. {ECO:0000250}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 250 314 {ECO:0000250}.
DISULFID 263 317 {ECO:0000250}.
DISULFID 351 367 {ECO:0000250}.
DISULFID 448 517 {ECO:0000250}.
DISULFID 480 496 {ECO:0000250}.
DISULFID 507 535 {ECO:0000250}.
VAR_SEQ 151 186 GTSLPKFTWREGQKQLPLIGCVLLLIALVVSLIILF -> V
(in isoform 3 and isoform 5).
{ECO:0000303|PubMed:11267681,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_013099.
VAR_SEQ 428 491 AHIHPACLPMHGQTFSLNETCWITGFGKTRETDDKTSPFLR
EVQVNLIDFKKCNDYLVYDSYLT -> GEGICTPRSPAPQP
QHPLQPSHLSASVNSYPGPKASAGQKSKTLKDPYMEHFCFI
IRETEAQGL (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_013100.
VAR_SEQ 492 586 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_013101.
VAR_SEQ 560 586 VRSLQQDTAPSRLGTSSGGDPGGAPRV -> SEVRFRKS
(in isoform 3).
{ECO:0000303|PubMed:11267681}.
/FTId=VSP_013102.
VAR_SEQ 560 563 VRSL -> SSAG (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_013103.
VAR_SEQ 564 586 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_013104.
CONFLICT 192 192 H -> Y (in Ref. 3; AAO38062).
{ECO:0000305}.
CONFLICT 206 206 K -> E (in Ref. 3; AAO38062).
{ECO:0000305}.
CONFLICT 211 211 C -> R (in Ref. 3; AAO38062).
{ECO:0000305}.
CONFLICT 510 510 D -> G (in Ref. 4; BAG62041).
{ECO:0000305}.
SEQUENCE 586 AA; 63153 MW; F842E3B7509FB1C6 CRC64;
MERDSHGNAS PARTPSAGAS PAQASPAGTP PGRASPAQAS PAQASPAGTP PGRASPAQAS
PAGTPPGRAS PGRASPAQAS PAQASPARAS PALASLSRSS SGRSSSARSA SVTTSPTRVY
LVRATPVGAV PIRSSPARSA PATRATRESP GTSLPKFTWR EGQKQLPLIG CVLLLIALVV
SLIILFQFWQ GHTGIRYKEQ RESCPKHAVR CDGVVDCKLK SDELGCVRFD WDKSLLKIYS
GSSHQWLPIC SSNWNDSYSE KTCQQLGFES AHRTTEVAHR DFANSFSILR YNSTIQESLH
RSECPSQRYI SLQCSHCGLR AMTGRIVGGA LASDSKWPWQ VSLHFGTTHI CGGTLIDAQW
VLTAAHCFFV TREKVLEGWK VYAGTSNLHQ LPEAASIAEI IINSNYTDEE DDYDIALMRL
SKPLTLSAHI HPACLPMHGQ TFSLNETCWI TGFGKTRETD DKTSPFLREV QVNLIDFKKC
NDYLVYDSYL TPRMMCAGDL RGGRDSCQGD SGGPLVCEQN NRWYLAGVTS WGTGCGQRNK
PGVYTKVTEV LPWIYSKMEV RSLQQDTAPS RLGTSSGGDP GGAPRV


Related products :

Catalog number Product name Quantity
EIAAB43244 Homo sapiens,Human,Membrane-type mosaic serine protease,Mosaic serine protease,MSP,TMPRSS11,TMPRSS13,Transmembrane protease serine 13
EIAAB43245 Membrane-type mosaic serine protease,Mosaic serine protease,Mouse,Msp,Mus musculus,Tmprss13,Transmembrane protease serine 13
EIAAB32605 Disp,Distal intestinal serine protease,Prss30,Rat,Rattus norvegicus,Serine protease 30,Tmprss8,Tmsp1,TMSP-1,Tmsp-1,Transmembrane serine protease 1,Transmembrane serine protease 8
EIAAB43231 CAPH2,Channel-activating protease 2,Homo sapiens,Human,Membrane-type serine protease 2,MT-SP2,TMPRSS3,TMPRSS4,Transmembrane protease serine 4,UNQ776_PRO1570
EIAAB40101 Homo sapiens,Human,Matriptase,Membrane-type serine protease 1,MT-SP1,Prostamin,PRSS14,Serine protease 14,Serine protease TADG-15,SNC19,ST14,Suppressor of tumorigenicity 14 protein,TADG15,Tumor-associa
EIAAB32606 Disp,Distal intestinal serine protease,Mouse,Mus musculus,Prss30,Serine protease 30,Tmprss8,Transmembrane serine protease 8
30-350 ST14 is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-pho 0.05 mg
EIAAB42596 DESC1,Homo sapiens,Human,Serine protease DESC1,TMPRSS11E,TMPRSS11E2,Transmembrane protease serine 11E,Transmembrane protease serine 11E2,UNQ742_PRO1461
EIAAB42593 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Rat,Rat,Rattus norvegicus,Tmprss11d,Transmembrane protease serine 11D
EIAAB42592 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Mat,Mouse,Mus musculus,Tmprss11d,Transmembrane protease serine 11D
U2234h CLIA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234h CLIA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2
E2234r ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234r CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234r ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234m ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
U2234m CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
U2234r CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234m CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
EIAAB42588 Airway trypsin-like protease 1,Desc3,DESC-3,Gm7,Hatl1,Mouse,Mus musculus,Serine protease DESC3,Tmprss11a,Transmembrane protease serine 11A
E2234m Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | 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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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