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

Stromelysin-3 (SL-3) (ST3) (EC 3.4.24.-) (Matrix metalloproteinase-11) (MMP-11)

 MMP11_HUMAN             Reviewed;         488 AA.
P24347; Q5FX24; Q6PEZ6; Q9UC26;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
20-JUN-2018, entry version 182.
RecName: Full=Stromelysin-3;
Short=SL-3;
Short=ST3;
EC=3.4.24.-;
AltName: Full=Matrix metalloproteinase-11;
Short=MMP-11;
Flags: Precursor;
Name=MMP11; Synonyms=STMY3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-38.
PubMed=1701851; DOI=10.1038/348699a0;
Basset P., Bellocq J.-P., Wolf C., Stoll I., Hutin P., Limacher J.-M.,
Podhajcer O.L., Chenard M.P., Rio M.C., Chambon P.;
"A novel metalloproteinase gene specifically expressed in stromal
cells of breast carcinomas.";
Nature 348:699-704(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-38; LYS-44; LEU-61
AND PRO-86.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-182.
TISSUE=Placenta;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
PubMed=7657606; DOI=10.1074/jbc.270.35.20337;
Anglard P., Melot T., Guerin E., Thomas G., Basset P.;
"Structure and promoter characterization of the human stromelysin-3
gene.";
J. Biol. Chem. 270:20337-20344(1995).
[6]
PROTEIN SEQUENCE OF 81-101.
PubMed=7746327; DOI=10.1038/375244a0;
Pei D., Weiss S.J.;
"Furin-dependent intracellular activation of the human stromelysin-3
zymogen.";
Nature 375:244-247(1995).
[7]
VARIANT [LARGE SCALE ANALYSIS] ASN-166.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: May play an important role in the progression of
epithelial malignancies.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- TISSUE SPECIFICITY: Specifically expressed in stromal cells of
breast carcinomas.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ST3ID200.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp11/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X57766; CAA40918.1; -; mRNA.
EMBL; AY899208; AAW65373.1; -; Genomic_DNA.
EMBL; AP000349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC057788; AAH57788.1; -; mRNA.
EMBL; X84664; CAA59150.1; -; Genomic_DNA.
CCDS; CCDS13816.1; -.
PIR; S13423; S13423.
RefSeq; NP_005931.2; NM_005940.4.
UniGene; Hs.143751; -.
ProteinModelPortal; P24347; -.
STRING; 9606.ENSP00000215743; -.
BindingDB; P24347; -.
ChEMBL; CHEMBL2867; -.
DrugBank; DB04318; 1-Benzyloxycarbonylamino-2-Phenyl-Ethyl)-{2-[1-Carbamoyl-2-(1h-Indol-3-Yl)-Ethylcarbamoyl]-5-Phenyl-Pentyl}-Phosphinic Acid.
DrugBank; DB00786; Marimastat.
GuidetoPHARMACOLOGY; 1635; -.
MEROPS; M10.007; -.
iPTMnet; P24347; -.
PhosphoSitePlus; P24347; -.
BioMuta; MMP11; -.
DMDM; 317373418; -.
PaxDb; P24347; -.
PeptideAtlas; P24347; -.
PRIDE; P24347; -.
ProteomicsDB; 54197; -.
Ensembl; ENST00000215743; ENSP00000215743; ENSG00000099953.
Ensembl; ENST00000612388; ENSP00000483349; ENSG00000275365.
GeneID; 4320; -.
KEGG; hsa:4320; -.
UCSC; uc002zxx.4; human.
CTD; 4320; -.
DisGeNET; 4320; -.
EuPathDB; HostDB:ENSG00000099953.9; -.
GeneCards; MMP11; -.
H-InvDB; HIX0203187; -.
HGNC; HGNC:7157; MMP11.
HPA; CAB002593; -.
HPA; HPA068864; -.
MIM; 185261; gene.
neXtProt; NX_P24347; -.
OpenTargets; ENSG00000099953; -.
PharmGKB; PA30869; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P24347; -.
KO; K07993; -.
OMA; HIWFFQG; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P24347; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.B3; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
ChiTaRS; MMP11; human.
GeneWiki; MMP11; -.
GenomeRNAi; 4320; -.
PRO; PR:P24347; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099953; -.
CleanEx; HS_MMP11; -.
ExpressionAtlas; P24347; baseline and differential.
Genevisible; P24347; HS.
GO; GO:0031012; C:extracellular matrix; IDA:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR028705; Stromelysin-3.
PANTHER; PTHR10201:SF20; PTHR10201:SF20; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Calcium; Cleavage on pair of basic residues; Collagen degradation;
Complete proteome; Direct protein sequencing; Disulfide bond;
Extracellular matrix; Hydrolase; Metal-binding; Metalloprotease;
Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal;
Zinc; Zymogen.
SIGNAL 1 31 {ECO:0000255}.
PROPEP 32 97 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028770.
CHAIN 98 488 Stromelysin-3.
/FTId=PRO_0000028771.
REPEAT 291 339 Hemopexin 1.
REPEAT 340 382 Hemopexin 2.
REPEAT 384 432 Hemopexin 3.
REPEAT 433 480 Hemopexin 4.
MOTIF 78 85 Cysteine switch. {ECO:0000250}.
ACT_SITE 216 216 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 80 80 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 166 166 Zinc 1. {ECO:0000250}.
METAL 171 171 Calcium. {ECO:0000250}.
METAL 172 172 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 174 174 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 176 176 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 179 179 Zinc 1. {ECO:0000250}.
METAL 192 192 Zinc 1. {ECO:0000250}.
METAL 215 215 Zinc 2; catalytic. {ECO:0000250}.
METAL 219 219 Zinc 2; catalytic. {ECO:0000250}.
METAL 225 225 Zinc 2; catalytic. {ECO:0000250}.
DISULFID 294 480 {ECO:0000250}.
VARIANT 38 38 A -> V (in dbSNP:rs738792).
{ECO:0000269|PubMed:1701851,
ECO:0000269|Ref.2}.
/FTId=VAR_022181.
VARIANT 44 44 E -> K (in dbSNP:rs28363646).
{ECO:0000269|Ref.2}.
/FTId=VAR_022182.
VARIANT 61 61 P -> L (in dbSNP:rs28363647).
{ECO:0000269|Ref.2}.
/FTId=VAR_022183.
VARIANT 86 86 S -> P (in dbSNP:rs28363648).
{ECO:0000269|Ref.2}.
/FTId=VAR_022184.
VARIANT 166 166 D -> N (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036140.
VARIANT 182 182 F -> S (in dbSNP:rs17854940).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_029659.
SEQUENCE 488 AA; 54590 MW; F03C537EE76706A9 CRC64;
MAPAAWLRSA AARALLPPML LLLLQPPPLL ARALPPDAHH LHAERRGPQP WHAALPSSPA
PAPATQEAPR PASSLRPPRC GVPDPSDGLS ARNRQKRFVL SGGRWEKTDL TYRILRFPWQ
LVQEQVRQTM AEALKVWSDV TPLTFTEVHE GRADIMIDFA RYWHGDDLPF DGPGGILAHA
FFPKTHREGD VHFDYDETWT IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR
YPLSLSPDDC RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA
VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA QGHIWFFQGA
QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI YFFRGRDYWR FHPSTRRVDS
PVPRRATDWR GVPSEIDAAF QDADGYAYFL RGRLYWKFDP VKVKALEGFP RLVGPDFFGC
AEPANTFL


Related products :

Catalog number Product name Quantity
10-664-50017 Stromelysin-3 - EC 3.4.24.-; ST3; SL-3; Matrix metalloproteinase-11; MMP-11 N_A 0.1 mg
GWB-9991FA Matrix Metalloproteinase-3 (MMP-3) Stromelysin-1 Ab-2, Antibody
15-288-21122 Stromelysin-3 - EC 3.4.24.-; ST3; SL-3; Matrix metalloproteinase-11; MMP-11 Polyclonal 0.1 mg
15-288-21122 Stromelysin-3 - EC 3.4.24.-; ST3; SL-3; Matrix metalloproteinase-11; MMP-11 Polyclonal 0.05 mg
Y103630 Matrix Metalloproteinase-3 (MMP-3), Stromelysin-1, Ab-2 Antibody 100ug
18-003-44329 Stromelysin-2 - EC 3.4.24.22; Matrix metalloproteinase-10; MMP-10; Transin-2; SL-2 Polyclonal 0.1 mg Protein A
E0224m ELISA Matrix metalloproteinase-11,Mmp11,MMP-11,Mouse,Mus musculus,SL-3,ST3,Stromelysin-3 96T
U0224r CLIA Matrix metalloproteinase-11,Mmp11,MMP-11,Rat,Rattus norvegicus,SL-3,ST3,Stromelysin-3 96T
U0224m CLIA Matrix metalloproteinase-11,Mmp11,MMP-11,Mouse,Mus musculus,SL-3,ST3,Stromelysin-3 96T
E0224r ELISA kit Matrix metalloproteinase-11,Mmp11,MMP-11,Rat,Rattus norvegicus,SL-3,ST3,Stromelysin-3 96T
E0224m ELISA kit Matrix metalloproteinase-11,Mmp11,MMP-11,Mouse,Mus musculus,SL-3,ST3,Stromelysin-3 96T
CSB-E04677h Human matrix metalloproteinase 3 per stromelysin 1(MMP3 per STR1) ELISA kit 96T
E0224r ELISA Matrix metalloproteinase-11,Mmp11,MMP-11,Rat,Rattus norvegicus,SL-3,ST3,Stromelysin-3 96T
E0098m ELISA Matrix metalloproteinase-10,Mmp10,MMP-10,Mouse,Mus musculus,SL-2,Stromelysin-2,Transin-2 96T
E0101m ELISA kit EMS-2,Matrix metalloproteinase-3,Mmp3,MMP-3,Mouse,Mus musculus,SL-1,Stromelysin-1,Transin-1 96T
E0098m ELISA kit Matrix metalloproteinase-10,Mmp10,MMP-10,Mouse,Mus musculus,SL-2,Stromelysin-2,Transin-2 96T
E0101m ELISA EMS-2,Matrix metalloproteinase-3,Mmp3,MMP-3,Mouse,Mus musculus,SL-1,Stromelysin-1,Transin-1 96T
U0098m CLIA Matrix metalloproteinase-10,Mmp10,MMP-10,Mouse,Mus musculus,SL-2,Stromelysin-2,Transin-2 96T
U0101m CLIA EMS-2,Matrix metalloproteinase-3,Mmp3,MMP-3,Mouse,Mus musculus,SL-1,Stromelysin-1,Transin-1 96T
EIAAB25019 Femalysin,Homo sapiens,Human,Matrix metalloproteinase-21,Matrix metalloproteinase-22,Matrix metalloproteinase-23,MIFR-1,MMP21,MMP-21,MMP-22,MMP-23,MMP23A
E0101Rb ELISA Matrix metalloproteinase-3,MMP3,MMP-3,Oryctolagus cuniculus,Rabbit,SL-1,Stromelysin-1,Transin-1 96T
E0224h ELISA Homo sapiens,Human,Matrix metalloproteinase-11,MMP11,MMP-11,SL-3,ST3,STMY3,Stromelysin-3 96T
E0101Rb ELISA kit Matrix metalloproteinase-3,MMP3,MMP-3,Oryctolagus cuniculus,Rabbit,SL-1,Stromelysin-1,Transin-1 96T
E0224h ELISA kit Homo sapiens,Human,Matrix metalloproteinase-11,MMP11,MMP-11,SL-3,ST3,STMY3,Stromelysin-3 96T
U0101Rb CLIA Matrix metalloproteinase-3,MMP3,MMP-3,Oryctolagus cuniculus,Rabbit,SL-1,Stromelysin-1,Transin-1 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