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

Inactive serine protease scarface

 SCARF_DROME             Reviewed;         655 AA.
Q7K5M0;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 1.
28-FEB-2018, entry version 121.
RecName: Full=Inactive serine protease scarface {ECO:0000303|PubMed:15342518, ECO:0000303|PubMed:20379222};
Flags: Precursor;
Name=scaf {ECO:0000303|PubMed:20530545,
ECO:0000312|FlyBase:FBgn0033033};
Synonyms=scarf {ECO:0000303|PubMed:20379222};
ORFNames=CG11066 {ECO:0000312|FlyBase:FBgn0033033};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000312|EMBL:AAK77280.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAK77280.1};
TISSUE=Head {ECO:0000312|EMBL:AAK77280.1};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4] {ECO:0000305}
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=15342518; DOI=10.1534/genetics.104.027557;
Bonin C.P., Mann R.S.;
"A piggyBac transposon gene trap for the analysis of gene expression
and function in Drosophila.";
Genetics 167:1801-1811(2004).
[5] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=20379222; DOI=10.1038/embor.2010.43;
Sorrosal G., Perez L., Herranz H., Milan M.;
"Scarface, a secreted serine protease-like protein, regulates
polarized localization of laminin A at the basement membrane of the
Drosophila embryo.";
EMBO Rep. 11:373-379(2010).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=20530545; DOI=10.1242/dev.050781;
Rousset R., Bono-Lauriol S., Gettings M., Suzanne M., Speder P.,
Noselli S.;
"The Drosophila serine protease homologue Scarface regulates JNK
signalling in a negative-feedback loop during epithelial
morphogenesis.";
Development 137:2177-2186(2010).
[7] {ECO:0000305}
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=25737837; DOI=10.1016/j.fob.2015.01.008;
Srivastava A., Dong Q.;
"Regulation of a serine protease homolog by the JNK pathway during
thoracic development of Drosophila melanogaster.";
FEBS Open Bio 5:117-123(2015).
[8] {ECO:0000305}
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=28628612; DOI=10.1371/journal.pgen.1006860;
Kushnir T., Mezuman S., Bar-Cohen S., Lange R., Paroush Z., Helman A.;
"Novel interplay between JNK and Egfr signaling in Drosophila dorsal
closure.";
PLoS Genet. 13:E1006860-E1006860(2017).
-!- FUNCTION: Inactive serine protease that plays a role in germ-band
retraction and dorsal closure morphogenesis in embryogenesis;
contributes to amnioserosa attachment and epithelial apico-basal
polarity by regulating the localization of laminin LanA on the
apical side of the amnioserosa epithelium (PubMed:28628612,
PubMed:20379222). Contributes to epithelial morphogenesis probably
by regulating the bsk/JNK pathway, as part of a negative-feedback
loop, and by modulating the cross-talk between the Egfr, bsk/JNK
and dpp signal transduction pathways (PubMed:28628612,
PubMed:20379222). In larval development, antagonizes the
morphogenetic movements controlled by the bsk/JNK signaling
including male genitalia formation and thorax development
(PubMed:20379222, PubMed:20530545, PubMed:25737837).
{ECO:0000269|PubMed:20379222, ECO:0000269|PubMed:20530545,
ECO:0000269|PubMed:25737837, ECO:0000269|PubMed:28628612}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15342518,
ECO:0000269|PubMed:20379222, ECO:0000269|PubMed:20530545}.
-!- DEVELOPMENTAL STAGE: In embryos, expressed in leading edge (LE)
cells (at protein level) (PubMed:20530545). In larvae, expressed
in the wing imaginal disk cells in the future hinge region,
specifically in the peripodial stalk and in the peripodial
membrane cells (at protein level) (PubMed:15342518,
PubMed:25737837). In larvae, expressed in the A8 abdomen-derived
cells in the male genital disk (at protein level)
(PubMed:20530545). In third instar larvae, expressed in the
anterior and posterios termini (at protein level)
(PubMed:15342518). In adult fly, expressed in the wing hinge, in
the socket cells of the micro- and macrochaete and proboscis (at
protein level) (PubMed:15342518). In embryos, expressed in leading
edge (LE) cells during germ-band retraction and dorsal closure
from stage 13; expressed in some cells of the amnioserosa in
particular in the posterior canthus as well as in the ventral
ectoderm; expressed both in head and tail region (PubMed:20379222,
PubMed:20530545, PubMed:28628612). {ECO:0000269|PubMed:15342518,
ECO:0000269|PubMed:20379222, ECO:0000269|PubMed:20530545,
ECO:0000269|PubMed:25737837, ECO:0000269|PubMed:28628612}.
-!- DOMAIN: The CLIP domain consists of 37-55 residues which are
"knitted" together usually by 3 conserved disulfide bonds forming
a clip-like compact structure. {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Embryonic lethal due to defects in the
dorsal closure and germ-band retraction; these defects include
undifferentiated or defective larval cuticles presenting dorsal
holes and wrinkles, defective attachment of the amnioserosa to the
tail end of the germ band, defective elongation of the lateral
ectoderm with compromised interface between the LE cells and the
amnioserosa (PubMed:20379222, PubMed:20530545, PubMed:15342518).
RNAi-mediated knockdown results in pupal lethality and scarring
(PubMed:25737837). RNAi-mediated knockdown in the epidermis
results in loss of wing veins and thorax mechanosensory bristles
as well as male terminalia malformations including genitalia
rotation defects and partial dissociation of the genital plate
from the abdomen (PubMed:20530545). RNAi-mediated knockdown in the
dorsal compartment of the wing disk results in loss of bristles
from the medio-lateral region of the thorax and in the appearance
of a mild thoracic cleft (PubMed:25737837). RNAi-mediated
knockdown in the notum area of the wing disk, destined to form the
dorsal medio-lateral region of the adult thorax as well as
thoracic bristles, results in a thoracic cleft and loss of
bristles from the medio-lateral region of the thorax
(PubMed:25737837). {ECO:0000269|PubMed:15342518,
ECO:0000269|PubMed:20379222, ECO:0000269|PubMed:20530545,
ECO:0000269|PubMed:25737837}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: Lacks the conserved residues within the catalytic triad,
probably resulting in a loss of proteolytic activity.
{ECO:0000303|PubMed:20379222}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AE013599; AAF57320.2; -; Genomic_DNA.
EMBL; AE013599; AAM68354.1; -; Genomic_DNA.
EMBL; AY047548; AAK77280.1; -; mRNA.
RefSeq; NP_610180.1; NM_136336.3.
RefSeq; NP_724424.1; NM_165441.2.
UniGene; Dm.7042; -.
SMR; Q7K5M0; -.
STRING; 7227.FBpp0085396; -.
EnsemblMetazoa; FBtr0086060; FBpp0085396; FBgn0033033.
EnsemblMetazoa; FBtr0086061; FBpp0085397; FBgn0033033.
GeneID; 35505; -.
KEGG; dme:Dmel_CG11066; -.
UCSC; CG11066-RA; d. melanogaster.
CTD; 35505; -.
FlyBase; FBgn0033033; scaf.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00770000120569; -.
OMA; ATKFDAC; -.
OrthoDB; EOG091G044M; -.
ChiTaRS; scaf; fly.
GenomeRNAi; 35505; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0033033; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:FlyBase.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
GO; GO:0007394; P:dorsal closure, elongation of leading edge cells; IMP:UniProtKB.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:UniProtKB.
GO; GO:0007390; P:germ-band shortening; IMP:UniProtKB.
GO; GO:0007560; P:imaginal disc morphogenesis; IMP:UniProtKB.
GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
GO; GO:0090099; P:negative regulation of decapentaplegic signaling pathway; IMP:UniProtKB.
GO; GO:0048802; P:notum morphogenesis; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; IEA:InterPro.
GO; GO:0050793; P:regulation of developmental process; IMP:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Disulfide bond;
Reference proteome; Secreted; Serine protease homolog; Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 655 Inactive serine protease scarface.
{ECO:0000255}.
/FTId=PRO_5010683600.
DOMAIN 343 407 CLIP. {ECO:0000255}.
DOMAIN 421 644 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
COMPBIAS 195 338 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
DISULFID 344 394 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 350 383 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 356 395 {ECO:0000250|UniProtKB:Q9VB68}.
DISULFID 450 466 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 547 605 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 579 587 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 595 623 {ECO:0000255|PROSITE-ProRule:PRU00274}.
SEQUENCE 655 AA; 71417 MW; 4726435D771ABF14 CRC64;
MSASHFREQL ALCITLAVLA AASGDYRANM FLNGQYQNGI KDQKENNLLV NPSTNVFLNH
AIISRQASPF QGPTYLPPKE FLKCAPGQQC VRSGQCLNGY FAQQLPKIQN CDPETTVCCT
YRPPPTTTTT TTTSVPVANC AYDSDCVTPD NCRNGEISAI NYVKKQGPNR CPAPNICCRI
PSTTLTEDGY IFNLPEKTFP LPTKPAVLAM PSTQAPFRPQ PTTAVPASRP TIEYLPPSTT
QHPSYEKVQT SRRPVYLPPS PATESASSLI PKIRPRPEPR PQPTRRPTNE YLPPAAANEI
PRFEPDRAPQ PSNQKPIYRG EDQLSPQIFP TPQPANVPKH FAKCASALVC TSENFCNAIG
VLSETPVELS PMEAAFRVPL TDCLQTENGS PGKCCRDPNY VDPWPVNLAG VCATRNKRTK
PTGVKDLDAN FAEIPWQAMI LRESSKTLIC GGAIIGDQFV LSSASCVNGL PVTDIRVKAG
EWELGSTNEP LPFQLTGVKT VDVHPDYDPS TNSHDLAIIR LERRLEFASH IQPICISDED
PKDSEQCFTS GWGKQALSIH EEGALMHVTD TLPQARSECS ADSSSVCSAT KFDSCQFDVG
SALACGSGSS VRLKGIFAGE NSCGEGQTVR FAKPDIKWIN TAFAENNKPL LLKRF


Related products :

Catalog number Product name Quantity
EIAAB32631 Inactive serine protease 45,Inactive testis serine protease 5,Mouse,Mus musculus,Prss45,Tessp5,Trypsin-like protease p98
EIAAB32634 Inactive serine protease 45,Inactive testis serine protease 5,Prss45,Rat,Rattus norvegicus,Tessp5
EIAAB32618 Inactive serine protease 39,Inactive testicular serine protease 1,Mouse,Mus musculus,Prss39,Tesp1
EIAAB32615 Homo sapiens,Human,Probable inactive serine protease 37,Probable inactive trypsin-X2,PRSS37,TRYX2
EIAAB32614 Mouse,Mus musculus,Probable inactive serine protease 37,Probable inactive trypsin-X2,Prss37,Tryx2
EIAAB32613 Bos taurus,Bovine,Probable inactive serine protease 37,Probable inactive trypsin-X2,PRSS37,TRYX2
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
ZN623_HUMAN Rat ELISA Kit FOR Inactive serine protease 54 96T
E0059m Rat ELISA Kit FOR Inactive serine protease 54 96T
CG033_HUMAN Rat ELISA Kit FOR Inactive serine protease 54 96T
EIAAB32606 Disp,Distal intestinal serine protease,Mouse,Mus musculus,Prss30,Serine protease 30,Tmprss8,Transmembrane serine protease 8
E0685b Bovine ELISA Kit FOR Inactive serine protease 35 96T
UBAD2_MOUSE Bovine ELISA Kit FOR Inactive serine protease 35 96T
SGIP1_HUMAN Human ELISA Kit FOR Inactive serine protease 54 96T
CSB-EL018822RA Rat Inactive serine protease 35(PRSS35) ELISA kit 96T
AT5F1_BOVIN Human ELISA Kit FOR Inactive serine protease 54 96T
E1685h Mouse ELISA Kit FOR Inactive serine protease 35 96T
E0095b Human ELISA Kit FOR Inactive serine protease 54 96T
PRS35_HUMAN Human ELISA Kit FOR Inactive serine protease 35 96T
E1635c Mouse ELISA Kit FOR Inactive serine protease 39 96T
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
EIAAB32609 Bos taurus,Bovine,Inactive serine protease 35,PRSS35
CSB-EL018822RA Rat Inactive serine protease 35(PRSS35) ELISA kit SpeciesRat 96T
ZBTB6_HUMAN Bovine ELISA Kit FOR Probable inactive serine protease 37 96T
EIAAB32610 Inactive serine protease 35,Prss35,Rat,Rattus norvegicus


 

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