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

Cruzipain (EC 3.4.22.51) (Cruzaine) (Major cysteine proteinase)

 CYSP_TRYCR              Reviewed;         467 AA.
P25779;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
30-AUG-2017, entry version 120.
RecName: Full=Cruzipain;
EC=3.4.22.51;
AltName: Full=Cruzaine;
AltName: Full=Major cysteine proteinase;
Flags: Precursor;
Trypanosoma cruzi.
Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
Schizotrypanum.
NCBI_TaxID=5693;
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=Tulahuen;
PubMed=1559982;
Eakin A.E., Mills A.A., Harth G., McKerrow J.H., Craik C.S.;
"The sequence, organization, and expression of the major cysteine
protease (cruzain) from Trypanosoma cruzi.";
J. Biol. Chem. 267:7411-7420(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONES 1800-2 AND 1800-4).
STRAIN=Tulahuen 2;
PubMed=1311053; DOI=10.1016/0166-6851(92)90219-A;
Campetella O., Henriksson J., Aaslund L., Frasch A.C.C.,
Pettersson U., Cazzulo J.J.;
"The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is
encoded by multiple polymorphic tandemly organized genes located on
different chromosomes.";
Mol. Biochem. Parasitol. 50:225-234(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-306.
STRAIN=RA;
PubMed=2406590; DOI=10.1016/0166-6851(90)90002-4;
Eakin A.E., Bouvier J., Sakanari J.A., Craik C.S., McKerrow J.H.;
"Amplification and sequencing of genomic DNA fragments encoding
cysteine proteases from protozoan parasites.";
Mol. Biochem. Parasitol. 39:1-8(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 295-467.
STRAIN=Tulahuen 2;
PubMed=2038364; DOI=10.1016/0166-6851(91)90103-D;
Aaslund L., Henriksson J., Campetella O., Frasch A.C.C.,
Pettersson U., Cazzulo J.J.;
"The C-terminal extension of the major cysteine proteinase (cruzipain)
from Trypanosoma cruzi.";
Mol. Biochem. Parasitol. 45:345-348(1991).
[5]
AUTOCATALYSIS OF C-TERMINAL.
STRAIN=Tulahuen 2;
PubMed=2011151; DOI=10.1016/0166-6851(91)90216-S;
Hellman U., Wernstedt C., Cazzulo J.J.;
"Self-proteolysis of the cysteine proteinase, cruzipain, from
Trypanosoma cruzi gives a major fragment corresponding to its carboxy-
terminal domain.";
Mol. Biochem. Parasitol. 44:15-21(1991).
[6]
SPECIFICITY.
STRAIN=Tulahuen 2;
PubMed=2407295; DOI=10.1016/0167-4838(90)90166-D;
Cazzulo J.J., Cazzulo-Franke M.C., Martinez J.,
Franke de Cazzulo B.M.;
"Some kinetic properties of a cysteine proteinase (cruzipain) from
Trypanosoma cruzi.";
Biochim. Biophys. Acta 1037:186-191(1990).
[7]
PROTEIN SEQUENCE OF 123-146 AND 304-317.
PubMed=2651912; DOI=10.1016/0166-6851(89)90039-X;
Cazzulo J.J., Couso R., Raimondi A., Wernstedt C., Hellman U.;
"Further characterization and partial amino acid sequence of a
cysteine proteinase from Trypanosoma cruzi.";
Mol. Biochem. Parasitol. 33:33-42(1989).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 123-337.
PubMed=9260273; DOI=10.1002/pro.5560060801;
Gillmor S.A., Craik C.S., Fletterick R.J.;
"Structural determinants of specificity in the cysteine protease
cruzain.";
Protein Sci. 6:1603-1611(1997).
-!- FUNCTION: Hydrolyzes chromogenic peptides at the carboxyl Arg or
Lys; requires at least one more amino acid, preferably Arg, Phe,
Val or Leu, between the terminal Arg or Lys and the amino-blocking
group.
-!- FUNCTION: The cysteine protease may play an important role in the
development and differentiation of the parasites at several stages
of their life cycle.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity similar to
that of cathepsin L.
-!- ENZYME REGULATION: Strongly inhibited by E-64 (L-trans-
epoxysuccinylleucylamido(4-guanidino)butane), Leupeptin, and N-
alpha-p-tosyl-L-lysine chloromethyl ketone.
-!- DEVELOPMENTAL STAGE: Present in all developmental stages.
-!- MISCELLANEOUS: Purified cruzipain is able to degrade itself,
yielding a complex mixture of small peptides, and a major 25 kDa
fragment.
-!- 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 http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M84342; AAA30181.1; -; Genomic_DNA.
EMBL; M69121; AAA30269.1; -; Genomic_DNA.
EMBL; M69121; AAA30270.1; -; Genomic_DNA.
EMBL; X54414; CAA38278.1; -; mRNA.
EMBL; M27305; AAA30180.1; -; Genomic_DNA.
PIR; A60667; A60667.
PIR; S16162; S16162.
PDB; 1AIM; X-ray; 2.00 A; A=123-337.
PDB; 1EWL; X-ray; 2.00 A; A=123-337.
PDB; 1EWM; X-ray; 2.00 A; A=123-337.
PDB; 1EWO; X-ray; 2.10 A; A=123-337.
PDB; 1EWP; X-ray; 1.75 A; A=123-337.
PDB; 1F29; X-ray; 2.15 A; A/B/C=123-337.
PDB; 1F2A; X-ray; 1.60 A; A=123-337.
PDB; 1F2B; X-ray; 1.80 A; A=123-337.
PDB; 1F2C; X-ray; 2.00 A; A=123-337.
PDB; 1ME3; X-ray; 1.20 A; A=123-337.
PDB; 1ME4; X-ray; 1.20 A; A=123-337.
PDB; 1U9Q; X-ray; 2.30 A; X=123-337.
PDB; 2AIM; X-ray; 2.20 A; A=123-337.
PDB; 2OZ2; X-ray; 1.95 A; A/C=123-337.
PDB; 3HD3; X-ray; 1.75 A; A/B=123-337.
PDB; 3I06; X-ray; 1.10 A; A=123-337.
PDB; 3IUT; X-ray; 1.20 A; A=123-337.
PDB; 3KKU; X-ray; 1.28 A; A=123-337.
PDB; 3LXS; X-ray; 1.50 A; A/C=123-337.
PDB; 4KLB; X-ray; 2.62 A; A/B/C/D/E=123-337.
PDB; 4PI3; X-ray; 1.27 A; A/B=122-337.
PDB; 4QH6; X-ray; 3.13 A; A/B/C/D/E=123-337.
PDB; 4W5B; X-ray; 2.70 A; A/B/C=123-337.
PDB; 4W5C; X-ray; 3.27 A; A/B/C/D/E=122-337.
PDB; 4XUI; X-ray; 2.51 A; A/B/C=122-337.
PDBsum; 1AIM; -.
PDBsum; 1EWL; -.
PDBsum; 1EWM; -.
PDBsum; 1EWO; -.
PDBsum; 1EWP; -.
PDBsum; 1F29; -.
PDBsum; 1F2A; -.
PDBsum; 1F2B; -.
PDBsum; 1F2C; -.
PDBsum; 1ME3; -.
PDBsum; 1ME4; -.
PDBsum; 1U9Q; -.
PDBsum; 2AIM; -.
PDBsum; 2OZ2; -.
PDBsum; 3HD3; -.
PDBsum; 3I06; -.
PDBsum; 3IUT; -.
PDBsum; 3KKU; -.
PDBsum; 3LXS; -.
PDBsum; 4KLB; -.
PDBsum; 4PI3; -.
PDBsum; 4QH6; -.
PDBsum; 4W5B; -.
PDBsum; 4W5C; -.
PDBsum; 4XUI; -.
ProteinModelPortal; P25779; -.
SMR; P25779; -.
BindingDB; P25779; -.
ChEMBL; CHEMBL3563; -.
DrugBank; DB04427; 3-[[N-[4-Methyl-Piperazinyl]Carbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonic Acid Benzyloxy-Amide.
DrugBank; DB02051; 3-[N-[Benzyloxycarbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonic Acid 4-Nitro-Phenyl Ester.
DrugBank; DB02200; 3-[N-[Benzyloxycarbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonylmethylbenzene.
DrugBank; DB01871; [1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester.
DrugBank; DB02128; [1-(3-Hydroxy-2-Oxo-1-Phenethyl-Propylcarbamoyl)2-Phenyl-Ethyl]-Carbamic Acid Pyridin-4-Ylmethyl Ester.
DrugBank; DB03536; Benzoyl-Arginine-Alanine-Methyl Ketone.
DrugBank; DB03691; WRR-112.
DrugBank; DB04502; WRR-204.
DrugBank; DB03573; WRR-99.
MEROPS; C01.075; -.
PaxDb; P25779; -.
eggNOG; KOG1542; Eukaryota.
eggNOG; COG4870; LUCA.
BRENDA; 3.4.22.51; 6524.
SABIO-RK; P25779; -.
EvolutionaryTrace; P25779; -.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
InterPro; IPR033163; CPB_peptidase.
InterPro; IPR021981; DUF3586.
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; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
PANTHER; PTHR12411:SF425; PTHR12411:SF425; 1.
Pfam; PF12131; DUF3586; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal;
Thiol protease; Zymogen.
SIGNAL 1 18 {ECO:0000305}.
PROPEP 19 122 Activation peptide.
{ECO:0000305|PubMed:2651912}.
/FTId=PRO_0000026372.
CHAIN 123 467 Cruzipain.
/FTId=PRO_0000026373.
ACT_SITE 147 147
ACT_SITE 284 284
ACT_SITE 304 304
SITE 337 338 Cleavage; by autolysis.
{ECO:0000269|PubMed:1559982}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 144 185
DISULFID 178 223
DISULFID 277 325
VARIANT 9 9 L -> S (in clone 1800-2).
VARIANT 35 35 T -> A (in clone 1800-2).
VARIANT 39 39 A -> V (in clone 1800-2).
VARIANT 51 51 S -> N (in clone 1800-4).
VARIANT 56 56 A -> R (in clone 1800-2).
VARIANT 76 76 N -> G (in clone 1800-4).
VARIANT 109 109 Q -> G (in clone 1800-4).
VARIANT 117 117 K -> N (in clone 1800-2).
VARIANT 146 146 S -> G.
VARIANT 157 158 EC -> SG (in strain: RA).
VARIANT 186 186 S -> G (in clones 1800-2 and 1800-4).
VARIANT 204 204 A -> G (in strain: RA).
VARIANT 250 251 WL -> CV (in clones 1800-2 and 1800-4).
VARIANT 261 262 VD -> H (in strain: RA).
VARIANT 286 286 V -> F (in clone 1800-4).
VARIANT 286 286 V -> L (in strain: RA).
VARIANT 308 308 T -> A (in clone 1800-2).
VARIANT 313 313 E -> D.
VARIANT 409 409 L -> F (in clone 1800-2).
VARIANT 427 427 K -> Q (in clone 1800-2).
VARIANT 430 430 R -> W (in clone 1800-2).
VARIANT 457 457 H -> Y (in clone 1800-2).
VARIANT 461 461 H -> Q (in clone 1800-2).
CONFLICT 357 357 S -> C (in Ref. 4). {ECO:0000305}.
STRAND 125 128 {ECO:0000244|PDB:3I06}.
HELIX 129 132 {ECO:0000244|PDB:3I06}.
STRAND 143 145 {ECO:0000244|PDB:4KLB}.
HELIX 147 162 {ECO:0000244|PDB:3I06}.
HELIX 172 178 {ECO:0000244|PDB:3I06}.
STRAND 180 182 {ECO:0000244|PDB:3I06}.
HELIX 184 186 {ECO:0000244|PDB:3I06}.
HELIX 190 200 {ECO:0000244|PDB:3I06}.
STRAND 204 207 {ECO:0000244|PDB:3I06}.
TURN 208 210 {ECO:0000244|PDB:3I06}.
STRAND 216 218 {ECO:0000244|PDB:2AIM}.
STRAND 225 227 {ECO:0000244|PDB:1F2A}.
STRAND 230 239 {ECO:0000244|PDB:3I06}.
HELIX 244 254 {ECO:0000244|PDB:3I06}.
STRAND 257 261 {ECO:0000244|PDB:3I06}.
HELIX 263 265 {ECO:0000244|PDB:4QH6}.
HELIX 266 268 {ECO:0000244|PDB:3I06}.
STRAND 271 274 {ECO:0000244|PDB:3I06}.
STRAND 284 297 {ECO:0000244|PDB:3I06}.
STRAND 299 303 {ECO:0000244|PDB:3I06}.
TURN 307 309 {ECO:0000244|PDB:4KLB}.
STRAND 315 322 {ECO:0000244|PDB:3I06}.
HELIX 324 326 {ECO:0000244|PDB:3I06}.
STRAND 329 336 {ECO:0000244|PDB:3I06}.
SEQUENCE 467 AA; 49836 MW; B93EBA49B511363D CRC64;
MSGWARALLL AAVLVVMACL VPAATASLHA EETLTSQFAE FKQKHGRVYE SAAEEAFRLS
VFRENLFLAR LHAAANPHAT FGVTPFSDLT REEFRSRYHN GAAHFAAAQE RARVPVKVEV
VGAPAAVDWR ARGAVTAVKD QGQCGSCWAF SAIGNVECQW FLAGHPLTNL SEQMLVSCDK
TDSGCSGGLM NNAFEWIVQE NNGAVYTEDS YPYASGEGIS PPCTTSGHTV GATITGHVEL
PQDEAQIAAW LAVNGPVAVA VDASSWMTYT GGVMTSCVSE QLDHGVLLVG YNDSAAVPYW
IIKNSWTTQW GEEGYIRIAK GSNQCLVKEE ASSAVVGGPG PTPEPTTTTT TSAPGPSPSY
FVQMSCTDAA CIVGCENVTL PTGQCLLTTS GVSAIVTCGA ETLTEEVFLT STHCSGPSVR
SSVPLNKCNR LLRGSVEFFC GSSSSGRLAD VDRQRRHQPY HSRHRRL


Related products :

Catalog number Product name Quantity
E0306m ELISA Cathepsin L1,Ctsl,Ctsl1,Major excreted protein,MEP,Mouse,Mus musculus,p39 cysteine proteinase 96T
E0306m ELISA kit Cathepsin L1,Ctsl,Ctsl1,Major excreted protein,MEP,Mouse,Mus musculus,p39 cysteine proteinase 96T
U0306m CLIA Cathepsin L1,Ctsl,Ctsl1,Major excreted protein,MEP,Mouse,Mus musculus,p39 cysteine proteinase 96T
20-321-175213 PROTEINASE 3 (PR3) - MONOCLONAL ANTIBODY TO HUMAN PROTEINASE 3 (PR3); EC 3.4.21.76; Leukocyte proteinase 3; PR-3; PR3; AGP7; Wegener autoantigen; P29; C-ANCA antigen; Neutrophil proteinase 4; NP-4 Mon 0.1 mg
gen5734 CATL1_MOUSE p39 cysteine proteinase ELISA tesk kit 1
Y052425 Anti-SERPINB12Serine or cysteine proteinase inhibitor clade B ovalbumin member 12 antibody 250ug
Y052425 Anti-SERPINB12(Serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 12) Antibody 100 μg
A167982 N-Acetyl-S-[3-acetamino-6-hydroxphenyl]cysteine-d5 Allyl Ester (Major) C16H15D5N2O5S CAS: 1331889-45-2 1 mg
10-002-38088 Vaspin. (21-414aa). Human. His-tagged.Recombinant. E Coli - SERPINA12; Serine (or cysteine) proteinase inhibitor. clade A; antitrypsin. alpha-1 antiproteinase; N_A N_A 0.5 mg
10-002-38088 Vaspin. (21-414aa). Human. His-tagged.Recombinant. E Coli - SERPINA12; Serine (or cysteine) proteinase inhibitor. clade A; antitrypsin. alpha-1 antiproteinase; N_A N_A 0.1 mg
31-063 Serine (or cysteine) proteinase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1) 0.1 mg
EIAAB30185 Homo sapiens,Human,PCOLCE,PCPE1,PCPE-1,Procollagen C-endopeptidase enhancer 1,Procollagen COOH-terminal proteinase enhancer 1,Procollagen C-proteinase enhancer 1,Type 1 procollagen C-proteinase enhanc
EIAAB30183 Mouse,Mus musculus,P14,Pcolce,Pcpe1,PCPE-1,Procollagen C-endopeptidase enhancer 1,Procollagen COOH-terminal proteinase enhancer 1,Procollagen C-proteinase enhancer 1,Type 1 procollagen C-proteinase en
EIAAB30184 Pcolce,Pcpe1,PCPE-1,Procollagen C-endopeptidase enhancer 1,Procollagen COOH-terminal proteinase enhancer 1,Procollagen C-proteinase enhancer 1,Rat,Rattus norvegicus,Type 1 procollagen C-proteinase enh
MAB - 606020373 Monoclonal Antibodies: Proteinase 3; reactive species: human; Clone: 3B4; Isotype: Mouse IgG2b; Specificity: Proteinase 3 0.1ml (1.0mg/ml)
EIAAB32680 AGP7,C-ANCA antigen,Homo sapiens,Human,Leukocyte proteinase 3,MBN,Myeloblastin,Neutrophil proteinase 4,NP-4,P29,PR3,PR-3,PRTN3,Wegener autoantigen
EIAAB09395 CRIPT,Cysteine-rich interactor of PDZ three,Cysteine-rich interactor of PDZ3,Cysteine-rich PDZ-binding protein,Homo sapiens,HSPC139,Human
orb82617 Human IGFBP3 protein IGFBP3 is a 30 kDa cysteine-rich secreted protein. It is the major IGF binding protein present in the plasma of human and animals and it is also found in alpha-granules of platele 5
EIAAB09391 Cript,Cysteine-rich interactor of PDZ three,Cysteine-rich interactor of PDZ3,Cysteine-rich PDZ-binding protein,Mouse,Mus musculus
EIAAB09393 Bos taurus,Bovine,CRIPT,Cysteine-rich interactor of PDZ three,Cysteine-rich interactor of PDZ3,Cysteine-rich PDZ-binding protein
EIAAB09394 Cript,Cysteine-rich interactor of PDZ three,Cysteine-rich interactor of PDZ3,Cysteine-rich PDZ-binding protein,Rat,Rattus norvegicus
18-003-43321 Cysteine protease ATG4B - EC 3.4.22.-; Autophagy-related protein 4 homolog B; hAPG4B; Autophagin-1; Autophagy-related cysteine endopeptidase 1; AUT-like 1 cysteine endopeptidase Polyclonal 0.05 mg Aff Pur
EIAAB32602 Implantation serine proteinase 1,Isp1,ISP-1,Mouse,Mus musculus,Prss28,Serine protease 28,Strypsin,Tryptase-like proteinase
orb90509 Proteinase K Proteinase K For research use only. 5 ml
EIAAB39439 Bos taurus,Bovine,Proteinase inhibitor 6,Serine proteinase inhibitor B-43,Serpin B6,SERPINB6


 

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