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

Alpha-crystallin (Acr) (14 kDa antigen) (16 kDa antigen) (HSP 16.3) (Nox16)

 ACR_MYCTU               Reviewed;         144 AA.
P9WMK1; L0TBA7; P0A5B7; P30223;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-MAR-2018, entry version 23.
RecName: Full=Alpha-crystallin;
Short=Acr;
AltName: Full=14 kDa antigen;
AltName: Full=16 kDa antigen;
AltName: Full=HSP 16.3;
AltName: Full=Nox16;
Name=hspX; Synonyms=acr; OrderedLocusNames=Rv2031c;
ORFNames=MTV018.18c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=1370952; DOI=10.1128/jb.174.4.1352-1359.1992;
Verbon A., Hartskeerl R.A., Schuitema A., Kolk A.H.J., Young D.B.,
Lathigra R.;
"The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is
related to the alpha-crystallin family of low-molecular-weight heat
shock proteins.";
J. Bacteriol. 174:1352-1359(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[3]
PROTEIN SEQUENCE OF 2-144, CHARACTERIZATION, SUBCELLULAR LOCATION, AND
MASS SPECTROMETRY.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=1563797;
Lee B.-Y., Hefta S.A., Brennan P.J.;
"Characterization of the major membrane protein of virulent
Mycobacterium tuberculosis.";
Infect. Immun. 60:2066-2074(1992).
[4]
PROTEIN SEQUENCE OF 2-13, AND INDUCTION BY NITRIC OXIDE (NO).
STRAIN=ATCC 25618 / H37Rv;
PubMed=9864257;
Garbe T.R., Hibler N.S., Deretic V.;
"Response to reactive nitrogen intermediates in Mycobacterium
tuberculosis: induction of the 16-kilodalton alpha-crystallin homolog
by exposure to nitric oxide donors.";
Infect. Immun. 67:460-465(1999).
[5]
FUNCTION AS A CHAPERONE, INDUCTION IN STATIONARY PHASE, AND INDUCTION
BY HYPOXIA.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=8755875; DOI=10.1128/jb.178.15.4484-4492.1996;
Yuan Y., Crane D.D., Barry C.E. III;
"Stationary phase-associated protein expression in Mycobacterium
tuberculosis: function of the mycobacterial alpha-crystallin
homolog.";
J. Bacteriol. 178:4484-4492(1996).
[6]
INDUCTION BY HYPOXIA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11416222; DOI=10.1073/pnas.121172498;
Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
Schoolnik G.K.;
"Regulation of the Mycobacterium tuberculosis hypoxic response gene
encoding alpha -crystallin.";
Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, MULTIPLE FORMS, AND INDUCTION BY
HYPOXIA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12057942; DOI=10.1128/JB.184.13.3485-3491.2002;
Rosenkrands I., Slayden R.A., Crawford J., Aagaard C., Barry C.E. III,
Andersen P.;
"Hypoxic response of Mycobacterium tuberculosis studied by metabolic
labeling and proteome analysis of cellular and extracellular
proteins.";
J. Bacteriol. 184:3485-3491(2002).
[8]
INDUCTION BY NITRIC OXIDE (NO); BY HYPOXIA; IN MOUSE MODEL AND
DORMANCY REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12953092; DOI=10.1084/jem.20030205;
Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I.,
Dolganov G.M., Sherman D.R., Schoolnik G.K.;
"Inhibition of respiration by nitric oxide induces a Mycobacterium
tuberculosis dormancy program.";
J. Exp. Med. 198:705-713(2003).
[9]
INDUCTION BY HOST IMMUNITY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12506197; DOI=10.1073/pnas.0136863100;
Shi L., Jung Y.J., Tyagi S., Gennaro M.L., North R.J.;
"Expression of Th1-mediated immunity in mouse lungs induces a
Mycobacterium tuberculosis transcription pattern characteristic of
nonreplicating persistence.";
Proc. Natl. Acad. Sci. U.S.A. 100:241-246(2003).
[10]
INDUCTION BY ANAEROBISIS, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=S-02293 Harlingen;
PubMed=15528667; DOI=10.1099/mic.0.27284-0;
Starck J., Kallenius G., Marklund B.I., Andersson D.I., Akerlund T.;
"Comparative proteome analysis of Mycobacterium tuberculosis grown
under aerobic and anaerobic conditions.";
Microbiology 150:3821-3829(2004).
[11]
DISRUPTION PHENOTYPE, AND PROBABLE OPERON STRUCTURE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16428728; DOI=10.1128/IAI.74.2.861-868.2006;
Hu Y., Movahedzadeh F., Stoker N.G., Coates A.R.;
"Deletion of the Mycobacterium tuberculosis alpha-crystallin-like hspX
gene causes increased bacterial growth in vivo.";
Infect. Immun. 74:861-868(2006).
[12]
BIOTECHNOLOGY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17145953; DOI=10.1128/IAI.01137-06;
Roupie V., Romano M., Zhang L., Korf H., Lin M.Y., Franken K.L.,
Ottenhoff T.H., Klein M.R., Huygen K.;
"Immunogenicity of eight dormancy regulon-encoded proteins of
Mycobacterium tuberculosis in DNA-vaccinated and tuberculosis-infected
mice.";
Infect. Immun. 75:941-949(2007).
[13]
INDUCTION BY CARBON MONOXIDE (CO).
STRAIN=ATCC 25618 / H37Rv;
PubMed=17609369; DOI=10.1073/pnas.0705054104;
Kumar A., Toledo J.C., Patel R.P., Lancaster J.R. Jr., Steyn A.J.;
"Mycobacterium tuberculosis DosS is a redox sensor and DosT is a
hypoxia sensor.";
Proc. Natl. Acad. Sci. U.S.A. 104:11568-11573(2007).
[14]
INDUCTION BY CARBON MONOXIDE (CO).
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
Shiloh M.U., Manzanillo P., Cox J.S.;
"Mycobacterium tuberculosis senses host-derived carbon monoxide during
macrophage infection.";
Cell Host Microbe 3:323-330(2008).
[15]
INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18400743; DOI=10.1074/jbc.M802274200;
Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S.,
Kramnik I., Agarwal A., Steyn A.J.;
"Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
tuberculosis dormancy regulon.";
J. Biol. Chem. 283:18032-18039(2008).
[16]
PUPYLATION AT LYS-64; LYS-85; LYS-114 AND LYS-132, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20066036; DOI=10.1371/journal.pone.0008589;
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
Gygi S.P., Darwin K.H.;
"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium
tuberculosis.";
PLoS ONE 5:E8589-E8589(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: Acts as a chaperone, as it has a significant ability to
suppress the thermal denaturation of alcohol dehydrogenase. Cells
overexpressing this gene grow more slowly than wild-type cells,
and are less susceptible to autolysis following saturation of the
culture in vitro, suggesting this protein may slow down the growth
rate of M.tuberculosis in culture and by extension during
macrophage infection. {ECO:0000269|PubMed:8755875}.
-!- INTERACTION:
P9WI75:pknF; NbExp=2; IntAct=EBI-2945921, EBI-2945875;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1563797}.
Secreted, cell wall {ECO:0000269|PubMed:1563797}. Note=Probably
the external side of the cell wall; the protein is very abundant
in older organisms and surface coating could be the result of
autolysis of older organisms.
-!- INDUCTION: Induced by several reactive nitrogen intermediates
including S-nitroso glutathione (at protein level). Induced in
stationary phase (at protein level). A member of the dormancy
regulon. Induced in response to reduced oxygen tension (hypoxia)
(at protein level), low levels of nitric oxide (NO) and carbon
monoxide (CO). It is hoped that this regulon will give insight
into the latent, or dormant phase of infection. Induced in mouse
lungs at the same time that adaptive host immunity induces
bacterial growth arrest; induction is dependent on interferon
gamma. A member of the probable hspX-Rv2030c-pfkB-Rv2028c operon.
{ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:12057942,
ECO:0000269|PubMed:12506197, ECO:0000269|PubMed:12953092,
ECO:0000269|PubMed:15528667, ECO:0000269|PubMed:17609369,
ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:18474359,
ECO:0000269|PubMed:8755875, ECO:0000269|PubMed:9864257}.
-!- PTM: Multiple forms of this protein exist in 2D-gels. The
differences between them has not been examined.
-!- MASS SPECTROMETRY: Mass=16100; Method=Electrospray; Range=2-144;
Evidence={ECO:0000269|PubMed:1563797};
-!- DISRUPTION PHENOTYPE: Strains deleted for this gene show
hypervirulence upon intravenous innoculation in BALB/c mice.
{ECO:0000269|PubMed:16428728}.
-!- BIOTECHNOLOGY: In plasmid DNA-vaccinated mice, subsequent
challenge with this protein induces positive levels of antigen-
specific IFN-gamma and IL-2, indicating this might be a good
vaccine candidate. {ECO:0000269|PubMed:17145953}.
-!- SIMILARITY: Belongs to the small heat shock protein (HSP20)
family. {ECO:0000255|PROSITE-ProRule:PRU00285}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; S79751; AAB21317.1; -; Genomic_DNA.
EMBL; M76712; AAA25342.1; -; Genomic_DNA.
EMBL; AL123456; CCP44804.1; -; Genomic_DNA.
PIR; F70942; F70942.
RefSeq; NP_216547.1; NC_000962.3.
RefSeq; WP_003410189.1; NZ_KK339370.1.
ProteinModelPortal; P9WMK1; -.
SMR; P9WMK1; -.
IntAct; P9WMK1; 6.
STRING; 83332.Rv2031c; -.
PaxDb; P9WMK1; -.
EnsemblBacteria; CCP44804; CCP44804; Rv2031c.
GeneID; 887579; -.
KEGG; mtu:Rv2031c; -.
TubercuList; Rv2031c; -.
eggNOG; COG0071; LUCA.
OMA; AGYDKGI; -.
PhylomeDB; P9WMK1; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0044183; F:protein binding involved in protein folding; IDA:MTBBASE.
GO; GO:0071456; P:cellular response to hypoxia; IEP:MTBBASE.
GO; GO:0009267; P:cellular response to starvation; IEP:MTBBASE.
GO; GO:0044121; P:growth of symbiont in host organelle; IMP:MTBBASE.
GO; GO:0045926; P:negative regulation of growth; IMP:MTBBASE.
GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
GO; GO:0006457; P:protein folding; IDA:MTBBASE.
GO; GO:0009408; P:response to heat; IDA:MTBBASE.
GO; GO:0075136; P:response to host; IEP:MTBBASE.
GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
GO; GO:0010039; P:response to iron ion; IEP:MTBBASE.
GO; GO:0051409; P:response to nitrosative stress; IEP:MTBBASE.
Gene3D; 2.60.40.790; -; 1.
InterPro; IPR002068; A-crystallin/Hsp20_dom.
InterPro; IPR008978; HSP20-like_chaperone.
Pfam; PF00011; HSP20; 1.
SUPFAM; SSF49764; SSF49764; 1.
PROSITE; PS01031; SHSP; 1.
1: Evidence at protein level;
Cell wall; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Reference proteome;
Secreted; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1563797,
ECO:0000269|PubMed:9864257}.
CHAIN 2 144 Alpha-crystallin.
/FTId=PRO_0000126011.
DOMAIN 33 143 sHSP. {ECO:0000255|PROSITE-
ProRule:PRU00285}.
CROSSLNK 64 64 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
CROSSLNK 85 85 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
CROSSLNK 114 114 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
CROSSLNK 132 132 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
SEQUENCE 144 AA; 16227 MW; A0C96872035CDDF8 CRC64;
MATTLPVQRH PRSLFPEFSE LFAAFPSFAG LRPTFDTRLM RLEDEMKEGR YEVRAELPGV
DPDKDVDIMV RDGQLTIKAE RTEQKDFDGR SEFAYGSFVR TVSLPVGADE DDIKATYDKG
ILTVSVAVSE GKPTEKHIQI RSTN


Related products :

Catalog number Product name Quantity
20-002-35008 alpha-Crystallin B (anti-human alpha-Crystallin B. clone 2E8) - Alpha(B)-crystallin; Rosenthal fiber component; Heat-shock protein beta-5; HspB5; NY-REN-27 antigen Monoclonal 0.1 ml
18-272-195324 alpha B Crystallin - Rabbit polyclonal to alpha B Crystallin; Alpha(B)-crystallin; Rosenthal fiber component; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27 Polyclonal 0.05 ml
18-272-195875 alpha B Crystallin - Rabbit polyclonal to alpha B Crystallin; Alpha(B)-crystallin; Rosenthal fiber component; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27 Polyclonal 0.1 ml
18-272-196324 alpha B Crystallin prediluted - Rabbit polyclonal to alpha B Crystallin prediluted; Alpha(B)-crystallin; Rosenthal fiber component; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27 7 ml
10-002-38007 Crystallin alpha B (CRYAB) - Alpha(B)-crystallin; Rosenthal fiber component; Heat-shock protein beta-5; HspB5; NY-REN-27 antigen N_A 1 mg
10-663-45483 Crystallin alpha B (CRYAB) Human - Alpha(B)-crystallin; Rosenthal fiber component; Heat-shock protein beta-5; HspB5; NY-REN-27 antigen N_A 0.1 mg
10-663-45483 Crystallin alpha B (CRYAB) Human - Alpha(B)-crystallin; Rosenthal fiber component; Heat-shock protein beta-5; HspB5; NY-REN-27 antigen N_A 1 mg
10-663-45483 Crystallin alpha B (CRYAB) Human - Alpha(B)-crystallin; Rosenthal fiber component; Heat-shock protein beta-5; HspB5; NY-REN-27 antigen N_A 0.02 mg
U0194h CLIA Alpha(B)-crystallin,Alpha-crystallin B chain,CRYA2,CRYAB,Heat shock protein beta-5,Homo sapiens,HspB5,Human,Renal carcinoma antigen NY-REN-27,Rosenthal fiber component 96T
E0194h ELISA kit Alpha(B)-crystallin,Alpha-crystallin B chain,CRYA2,CRYAB,Heat shock protein beta-5,Homo sapiens,HspB5,Human,Renal carcinoma antigen NY-REN-27,Rosenthal fiber component 96T
E0194h ELISA Alpha(B)-crystallin,Alpha-crystallin B chain,CRYA2,CRYAB,Heat shock protein beta-5,Homo sapiens,HspB5,Human,Renal carcinoma antigen NY-REN-27,Rosenthal fiber component 96T
'AR03037PU-L Alpha-crystallin A chain (1-175) antigen 0.5 mg
'AR03037PU-N Alpha-crystallin A chain (1-175) antigen 0.1 mg
SA6019X Alpha-crystallin B chain antigen Purified 1 mg
SA6018 Alpha-crystallin A chain antigen Purified 0.1 mg
SA6018X Alpha-crystallin A chain antigen Purified 1 mg
SA6019 Alpha-crystallin B chain antigen Purified 0.1 mg
15-288-21349 Integrin alpha-E - Mucosal lymphocyte 1 antigen; HML-1 antigen; Integrin alpha-IEL; CD103 antigen Polyclonal 0.05 mg
15-288-21349 Integrin alpha-E - Mucosal lymphocyte 1 antigen; HML-1 antigen; Integrin alpha-IEL; CD103 antigen Polyclonal 0.1 mg
ITGAM ITGAE Gene integrin, alpha E (antigen CD103, human mucosal lymphocyte antigen 1; alpha polypeptide)
ITGAV ITGAL Gene integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)
X2183P Human Integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor) (ITGA4) Antigen Immunoaffinity Purified Polyclonal 50
X2176P Human Integrin, Alpha X (Antigen CD11C (P150), Alpha Polypeptide) (ITGAX) Antigen Immunoaffinity Purified Polyclonal 50
X2174P Human Integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor) (ITGA4) Antigen Immunoaffinity Purified Polyclonal 50
X2175P Human Integrin, Alpha X (Antigen CD11C (P150), Alpha Polypeptide) (ITGAX) Antigen Immunoaffinity Purified Polyclonal 50


 

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