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

Cathepsin B (EC 3.4.22.1) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain]

 CATB_MOUSE              Reviewed;         339 AA.
P10605; Q3UDW7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
12-SEP-2018, entry version 178.
RecName: Full=Cathepsin B;
EC=3.4.22.1;
AltName: Full=Cathepsin B1;
Contains:
RecName: Full=Cathepsin B light chain;
Contains:
RecName: Full=Cathepsin B heavy chain;
Flags: Precursor;
Name=Ctsb;
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.
PubMed=2012677; DOI=10.1089/dna.1991.10.159;
Qian F., Frankfater A., Chan S.J., Steiner D.F.;
"The structure of the mouse cathepsin B gene and its putative
promoter.";
DNA Cell Biol. 10:159-168(1991).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=2226854; DOI=10.1016/0014-5793(90)81083-Z;
Ferrara M., Wojcik F., Rhaissi H., Mordier S., Roux M.-P., Bechet D.;
"Gene structure of mouse cathepsin B.";
FEBS Lett. 273:195-199(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3463996; DOI=10.1073/pnas.83.20.7721;
Chan S.J., San Segundo B., McCormick M.B., Steiner D.F.;
"Nucleotide and predicted amino acid sequences of cloned human and
mouse preprocathepsin B cDNAs.";
Proc. Natl. Acad. Sci. U.S.A. 83:7721-7725(1986).
[4]
NUCLEOTIDE SEQUENCE.
PubMed=1746902;
Qian F., Frankfater A., Steiner D.F., Bajkowski A.S., Chan S.J.;
"Characterization of multiple cathepsin B mRNAs in murine B16a
melanoma.";
Anticancer Res. 11:1445-1451(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Placenta, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 314-339.
PubMed=1889751; DOI=10.1016/0378-1119(91)90283-H;
Friemert C., Closs E.I., Silbermann M., Erfle V., Strauss P.G.;
"Isolation of a cathepsin B-encoding cDNA from murine osteogenic
cells.";
Gene 103:259-261(1991).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Thiol protease which is believed to participate in
intracellular degradation and turnover of proteins. Has also been
implicated in tumor invasion and metastasis.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity
for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in
small molecule substrates (thus differing from cathepsin L). In
addition to being an endopeptidase, shows peptidyl-dipeptidase
activity, liberating C-terminal dipeptides.
-!- SUBUNIT: Interacts with SRPX2 (By similarity). Dimer of a heavy
chain and a light chain cross-linked by a disulfide bond. Directly
interacts with SHKBP1 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P07858}.
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07858}.
Melanosome {ECO:0000250}. Secreted, extracellular space
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M65270; AAA37375.1; -; Genomic_DNA.
EMBL; M65263; AAA37375.1; JOINED; Genomic_DNA.
EMBL; M65264; AAA37375.1; JOINED; Genomic_DNA.
EMBL; M65265; AAA37375.1; JOINED; Genomic_DNA.
EMBL; M65266; AAA37375.1; JOINED; Genomic_DNA.
EMBL; M65267; AAA37375.1; JOINED; Genomic_DNA.
EMBL; M65268; AAA37375.1; JOINED; Genomic_DNA.
EMBL; M65269; AAA37375.1; JOINED; Genomic_DNA.
EMBL; M14222; AAA37494.1; -; mRNA.
EMBL; X54966; CAA38713.1; -; mRNA.
EMBL; S69034; AAB20536.1; -; mRNA.
EMBL; AK083393; BAC38900.1; -; mRNA.
EMBL; AK147192; BAE27751.1; -; mRNA.
EMBL; AK149884; BAE29144.1; -; mRNA.
EMBL; AK151790; BAE30691.1; -; mRNA.
EMBL; AK167361; BAE39458.1; -; mRNA.
EMBL; BC006656; AAH06656.1; -; mRNA.
CCDS; CCDS27197.1; -.
PIR; A38458; KHMSB.
RefSeq; NP_031824.1; NM_007798.3.
UniGene; Mm.236553; -.
ProteinModelPortal; P10605; -.
SMR; P10605; -.
BioGrid; 198968; 3.
ComplexPortal; CPX-100; Cathepsin-B - cystatin-A complex.
IntAct; P10605; 9.
MINT; P10605; -.
STRING; 10090.ENSMUSP00000006235; -.
BindingDB; P10605; -.
ChEMBL; CHEMBL5187; -.
MEROPS; C01.060; -.
iPTMnet; P10605; -.
PhosphoSitePlus; P10605; -.
SwissPalm; P10605; -.
SWISS-2DPAGE; P10605; -.
EPD; P10605; -.
MaxQB; P10605; -.
PaxDb; P10605; -.
PeptideAtlas; P10605; -.
PRIDE; P10605; -.
Ensembl; ENSMUST00000006235; ENSMUSP00000006235; ENSMUSG00000021939.
GeneID; 13030; -.
KEGG; mmu:13030; -.
UCSC; uc007uhh.2; mouse.
CTD; 1508; -.
MGI; MGI:88561; Ctsb.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140859; -.
HOGENOM; HOG000241341; -.
HOVERGEN; HBG003480; -.
InParanoid; P10605; -.
KO; K01363; -.
OMA; HCGIESS; -.
OrthoDB; EOG091G094Z; -.
PhylomeDB; P10605; -.
TreeFam; TF314576; -.
BioCyc; MetaCyc:MONOMER-14810; -.
BRENDA; 3.4.22.1; 3474.
BRENDA; 3.4.23.5; 3474.
Reactome; R-MMU-1442490; Collagen degradation.
Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Ctsb; mouse.
PRO; PR:P10605; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000021939; Expressed in 320 organ(s), highest expression level in stroma of bone marrow.
CleanEx; MM_CTSB; -.
Genevisible; P10605; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0042383; C:sarcolemma; ISO:MGI.
GO; GO:0005518; F:collagen binding; ISO:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
GO; GO:0030984; F:kininogen binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0042277; F:peptide binding; ISO:MGI.
GO; GO:0043621; F:protein self-association; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
GO; GO:0046697; P:decidualization; IGI:MGI.
GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IMP:CACAO.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR012599; Propeptide_C1A.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF00112; Peptidase_C1; 1.
Pfam; PF08127; Propeptide_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Lysosome; Protease; Reference proteome; Secreted; Signal;
Thiol protease; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 79 Activation peptide.
/FTId=PRO_0000026148.
CHAIN 80 333 Cathepsin B.
/FTId=PRO_0000026149.
CHAIN 80 126 Cathepsin B light chain. {ECO:0000250}.
/FTId=PRO_0000026150.
CHAIN 129 333 Cathepsin B heavy chain. {ECO:0000250}.
/FTId=PRO_0000026151.
PROPEP 334 339 {ECO:0000250}.
/FTId=PRO_0000026152.
ACT_SITE 108 108 {ECO:0000250}.
ACT_SITE 278 278 {ECO:0000250}.
ACT_SITE 298 298 {ECO:0000250}.
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 93 122 {ECO:0000250}.
DISULFID 105 150 {ECO:0000250}.
DISULFID 141 207 {ECO:0000250}.
DISULFID 142 146 {ECO:0000250}.
DISULFID 179 211 {ECO:0000250}.
DISULFID 187 198 {ECO:0000250}.
CONFLICT 160 160 S -> N (in Ref. 3; AAA37494).
{ECO:0000305}.
CONFLICT 174 174 N -> D (in Ref. 3; AAA37494).
{ECO:0000305}.
CONFLICT 177 177 V -> I (in Ref. 3; AAA37494).
{ECO:0000305}.
CONFLICT 284 284 G -> V (in Ref. 3; AAA37494).
{ECO:0000305}.
SEQUENCE 339 AA; 37280 MW; 9F0A3CDF70A94040 CRC64;
MWWSLILLSC LLALTSAHDK PSFHPLSDDL INYINKQNTT WQAGRNFYNV DISYLKKLCG
TVLGGPKLPG RVAFGEDIDL PETFDAREQW SNCPTIGQIR DQGSCGSCWA FGAVEAISDR
TCIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWS FWTKKGLVSG GVYNSHVGCL
PYTIPPCEHH VNGSRPPCTG EGDTPRCNKS CEAGYSPSYK EDKHFGYTSY SVSNSVKEIM
AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDMMGGHAI RILGWGVENG VPYWLAANSW
NLDWGDNGFF KILRGENHCG IESEIVAGIP RTDQYWGRF


Related products :

Catalog number Product name Quantity
E0267h ELISA kit Cathepsin K,Cathepsin O,Cathepsin O2,Cathepsin X,CTSK,CTSO,CTSO2,Homo sapiens,Human 96T
E0267h ELISA Cathepsin K,Cathepsin O,Cathepsin O2,Cathepsin X,CTSK,CTSO,CTSO2,Homo sapiens,Human 96T
U0267h CLIA Cathepsin K,Cathepsin O,Cathepsin O2,Cathepsin X,CTSK,CTSO,CTSO2,Homo sapiens,Human 96T
EIAAB05436 Cathepsin L2,Cathepsin U,Cathepsin V,CATL2,CTSL2,CTSU,CTSV,Homo sapiens,Human,UNQ268_PRO305
EIAAB05433 Cathepsin J,Cathepsin L-related protein,Cathepsin P,Catlrp-p,Ctsj,Ctsp,Rat,Rattus norvegicus
EIAAB05434 Cathepsin J,Cathepsin L-related protein,Cathepsin P,Catlrp-p,Ctsj,Ctsp,Mouse,Mus musculus
3741BP-50 Cathepsin L (Cleaved) Blocking Peptide target: Cathepsin L (Cleaved) 50 μg
EIAAB05448 Cathepsin P,Cathepsin X,Cathepsin Z,CTSZ,Homo sapiens,Human
3741BP-50 Cathepsin L (Cleaved) Blocking Peptide Cathepsin 50 μg
EIAAB05431 Cathepsin B3,Cathepsin BA,Ctsh,Mouse,Mus musculus,Pro-cathepsin H
orb90060 Human Cathepsin L protein Cathepsin Human Recombinant (aa 1-87) expressed in E.coli, shows 38 kDa band on SDS-PAGE.The Cathepsin is purified by proprietary chromatographic techniques. For research use 2
10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 0.01 mg
10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 0.002 mg
10-663-45680 Procathepsin K Human - EC 3.4.22.38; Cathepsin O; Cathepsin X; Cathepsin O2 N_A 1 mg
BM773 Cathepsin D (167_181 heavy chain) 0.2 mg
BM773 Cathepsin D (167_181 heavy chain) 0.2 mg
BM773 Cathepsin D (167_181 heavy chain) 0.2 mg
18-272-196838 Cathepsin B - Sheep polyclonal to Cathepsin B; EC 3.4.22.1; Cathepsin B1; APP secretase; APPS Polyclonal 1 ml
NB100-62441 Cathepsin D (167_181 heavy chain) 0.2 mg
NB100-62441 Cathepsin D (167_181 heavy chain) 0.2 mg
20-783-73093 MOUSE ANTI HUMAN CATHEPSIN D HEAVY CHAIN - EC 3.4.23.5 Monoclonal 0.2 mg
6202 Cathepsin B (Human Liver), purified cathepsin and related proteases 25
6205 Cathepsin H (Human Liver), purified cathepsin and related proteases 25
6206 Cathepsin L (Human Liver), purified cathepsin and related proteases 25
6203 Cathepsin D (Human Liver), purified cathepsin and related proteases 25


 

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