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

T-cell surface glycoprotein CD4 (T-cell surface antigen T4/Leu-3) (W3/25 antigen) (CD antigen CD4)

 CD4_RAT                 Reviewed;         457 AA.
P05540;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=T-cell surface glycoprotein CD4;
AltName: Full=T-cell surface antigen T4/Leu-3;
AltName: Full=W3/25 antigen;
AltName: CD_antigen=CD4;
Flags: Precursor;
Name=Cd4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3104900; DOI=10.1073/pnas.84.6.1649;
Clark S.J., Jefferies W.A., Barclay A.N., Gagnon J., Williams A.F.;
"Peptide and nucleotide sequences of rat CD4 (W3/25) antigen: evidence
for derivation from a structure with four immunoglobulin-related
domains.";
Proc. Natl. Acad. Sci. U.S.A. 84:1649-1653(1987).
[2]
PROTEIN SEQUENCE OF 42-51; 83-88; 95-101; 109-112; 146-164; 178-192;
256-273; 292-300; 327-329 AND 368-371, DISULFIDE BONDS, GLYCOSYLATION
AT ASN-186 AND ASN-297, AND MUTAGENESIS OF ASN-186 AND ASN-297.
PubMed=2113054;
Davis S.J., Ward H.A., Puklavec M.J., Willis A.C., Williams A.F.,
Barclay A.N.;
"High level expression in Chinese hamster ovary cells of soluble forms
of CD4 T lymphocyte glycoprotein including glycosylation variants.";
J. Biol. Chem. 265:10410-10418(1990).
[3]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-393.
PubMed=8493535; DOI=10.1126/science.8493535;
Brady R.L., Dodson E.J., Dodson G.G., Lange G., Davis S.J.,
Williams A.F., Barclay A.N.;
"Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-
terminal domains.";
Science 260:979-983(1993).
-!- FUNCTION: Integral membrane glycoprotein that plays an essential
role in the immune response and serves multiple functions in
responses against both external and internal offenses. In T-cells,
functions primarily as a coreceptor for MHC class II
molecule:peptide complex. The antigens presented by class II
peptides are derived from extracellular proteins while class I
peptides are derived from cytosolic proteins. Interacts
simultaneously with the T-cell receptor (TCR) and the MHC class II
presented by antigen presenting cells (APCs). In turn, recruits
the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK
then initiates different intracellular signaling pathways by
phosphorylating various substrates ultimately leading to
lymphokine production, motility, adhesion and activation of T-
helper cells. In other cells such as macrophages or NK cells,
plays a role in differentiation/activation, cytokine expression
and cell migration in a TCR/LCK-independent pathway. Participates
in the development of T-helper cells in the thymus and triggers
the differentiation of monocytes into functional mature
macrophages. {ECO:0000250|UniProtKB:P01730}.
-!- SUBUNIT: Forms disulfide-linked homo-dimers at the cell surface.
Interacts with LCK. Interacts with PTK2/FAK1. Binds to P4HB/PDI.
Interacts with IL16; this interaction induces a CD4-dependent
signaling in lymphocytes. {ECO:0000250|UniProtKB:P01730}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P01730}. Note=Localizes to lipid
rafts. {ECO:0000250|UniProtKB:P01730}.
-!- PTM: Palmitoylation and association with LCK contribute to the
enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}.
-!- PTM: Phosphorylated by PKC; phosphorylation plays an important
role for CD4 internalization. {ECO:0000250|UniProtKB:P01730}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M15768; AAA40901.1; -; mRNA.
PIR; A27449; A27449.
RefSeq; NP_036837.1; NM_012705.1.
RefSeq; XP_006237393.1; XM_006237331.3.
RefSeq; XP_008761502.1; XM_008763280.2.
UniGene; Rn.10748; -.
PDB; 1CID; X-ray; 2.80 A; A=210-386.
PDBsum; 1CID; -.
ProteinModelPortal; P05540; -.
SMR; P05540; -.
MINT; MINT-4996350; -.
STRING; 10116.ENSRNOP00000021915; -.
iPTMnet; P05540; -.
UniCarbKB; P05540; -.
PaxDb; P05540; -.
PRIDE; P05540; -.
Ensembl; ENSRNOT00000021915; ENSRNOP00000021915; ENSRNOG00000016294.
GeneID; 24932; -.
KEGG; rno:24932; -.
UCSC; RGD:2306; rat.
CTD; 920; -.
RGD; 2306; Cd4.
eggNOG; ENOG410IK9F; Eukaryota.
eggNOG; ENOG410YWI4; LUCA.
GeneTree; ENSGT00390000001745; -.
HOGENOM; HOG000008696; -.
HOVERGEN; HBG005281; -.
InParanoid; P05540; -.
KO; K06454; -.
OMA; PEAGMWQ; -.
OrthoDB; EOG091G0AZL; -.
PhylomeDB; P05540; -.
TreeFam; TF335974; -.
Reactome; R-RNO-1462054; Alpha-defensins.
Reactome; R-RNO-202424; Downstream TCR signaling.
Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-RNO-202433; Generation of second messenger molecules.
Reactome; R-RNO-389948; PD-1 signaling.
Reactome; R-RNO-449836; Other interleukin signaling.
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
EvolutionaryTrace; P05540; -.
PRO; PR:P05540; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000016294; -.
Genevisible; P05540; RN.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0019865; F:immunoglobulin binding; IDA:RGD.
GO; GO:0042011; F:interleukin-16 binding; ISO:RGD.
GO; GO:0042012; F:interleukin-16 receptor activity; ISO:RGD.
GO; GO:0042289; F:MHC class II protein binding; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:1990782; F:protein tyrosine kinase binding; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISO:RGD.
GO; GO:0001816; P:cytokine production; ISO:RGD.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
GO; GO:0035397; P:helper T cell enhancement of adaptive immune response; ISO:RGD.
GO; GO:0006948; P:induction by virus of host cell-cell fusion; ISO:RGD.
GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:RGD.
GO; GO:0032507; P:maintenance of protein location in cell; ISO:RGD.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:RGD.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
GO; GO:0033674; P:positive regulation of kinase activity; ISO:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
GO; GO:0045657; P:positive regulation of monocyte differentiation; ISO:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:0050870; P:positive regulation of T cell activation; ISO:RGD.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:RGD.
GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
GO; GO:0050863; P:regulation of T cell activation; ISO:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
GO; GO:0042110; P:T cell activation; IMP:RGD.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0045058; P:T cell selection; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR000973; CD4.
InterPro; IPR015274; CD4-extracel.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR008424; Ig_C2-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR021963; Tcell_CD4_Cterm.
PANTHER; PTHR11422:SF0; PTHR11422:SF0; 1.
Pfam; PF05790; C2-set; 2.
Pfam; PF09191; CD4-extracel; 1.
Pfam; PF00047; ig; 1.
Pfam; PF12104; Tcell_CD4_C; 1.
PRINTS; PR00692; CD4TCANTIGEN.
SMART; SM00409; IG; 3.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 27
CHAIN 28 457 T-cell surface glycoprotein CD4.
/FTId=PRO_0000014629.
TOPO_DOM 28 394 Extracellular. {ECO:0000255}.
TRANSMEM 395 417 Helical. {ECO:0000255}.
TOPO_DOM 418 457 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 127 Ig-like V-type.
DOMAIN 128 206 Ig-like C2-type 1.
DOMAIN 207 316 Ig-like C2-type 2.
DOMAIN 317 374 Ig-like C2-type 3.
LIPID 418 418 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 421 421 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2113054}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2113054}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 43 111 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:2113054}.
DISULFID 158 187 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:2113054}.
DISULFID 328 370 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:2113054}.
MUTAGEN 186 186 N->T: No change in secretion; when
associated with S-297.
{ECO:0000269|PubMed:2113054}.
MUTAGEN 297 297 N->S: No change in secretion; when
associated with T-186.
{ECO:0000269|PubMed:2113054}.
STRAND 213 217 {ECO:0000244|PDB:1CID}.
STRAND 222 225 {ECO:0000244|PDB:1CID}.
STRAND 235 245 {ECO:0000244|PDB:1CID}.
STRAND 252 258 {ECO:0000244|PDB:1CID}.
STRAND 261 266 {ECO:0000244|PDB:1CID}.
STRAND 282 285 {ECO:0000244|PDB:1CID}.
HELIX 290 292 {ECO:0000244|PDB:1CID}.
STRAND 294 301 {ECO:0000244|PDB:1CID}.
STRAND 303 319 {ECO:0000244|PDB:1CID}.
STRAND 321 332 {ECO:0000244|PDB:1CID}.
STRAND 336 344 {ECO:0000244|PDB:1CID}.
STRAND 349 362 {ECO:0000244|PDB:1CID}.
STRAND 365 374 {ECO:0000244|PDB:1CID}.
STRAND 377 385 {ECO:0000244|PDB:1CID}.
SEQUENCE 457 AA; 51438 MW; 477BE157D30954C1 CRC64;
MCRGFSFRHL LPLLLLQLSK LLVVTQGKTV VLGKEGGSAE LPCESTSRRS ASFAWKSSDQ
KTILGYKNKL LIKGSLELYS RFDSRKNAWE RGSFPLIINK LRMEDSQTYV CELENKKEEV
ELWVFRVTFN PGTRLLQGQS LTLILDSNPK VSDPPIECKH KSSNIVKDSK AFSTHSLRIQ
DSGIWNCTVT LNQKKHSFDM KLSVLGFAST SITAYKSEGE SAEFSFPLNL GEESLQGELR
WKAEKAPSSQ SWITFSLKNQ KVSVQKSTSN PKFQLSETLP LTLQIPQVSL QFAGSGNLTL
TLDRGILYQE VNLVVMKVTQ PDSNTLTCEV MGPTSPKMRL ILKQENQEAR VSRQEKVIQV
QAPEAGVWQC LLSEGEEVKM DSKIQVLSKG LNQTMFLAVV LGSAFSFLVF TGLCILFCVR
CRHQQRQAAR MSQIKRLLSE KKTCQCSHRM QKSHNLI


Related products :

Catalog number Product name Quantity
U1014m CLIA Cd4,Mouse,Mus musculus,T-cell differentiation antigen L3T4,T-cell surface antigen T4_Leu-3,T-cell surface glycoprotein CD4 96T
E1014m ELISA Cd4,Mouse,Mus musculus,T-cell differentiation antigen L3T4,T-cell surface antigen T4_Leu-3,T-cell surface glycoprotein CD4 96T
E1014m ELISA kit Cd4,Mouse,Mus musculus,T-cell differentiation antigen L3T4,T-cell surface antigen T4_Leu-3,T-cell surface glycoprotein CD4 96T
E1014r ELISA kit Cd4,Rat,Rattus norvegicus,T-cell surface antigen T4_Leu-3,T-cell surface glycoprotein CD4,W3_25 antigen 96T
U1014r CLIA Cd4,Rat,Rattus norvegicus,T-cell surface antigen T4_Leu-3,T-cell surface glycoprotein CD4,W3_25 antigen 96T
E1014r ELISA Cd4,Rat,Rattus norvegicus,T-cell surface antigen T4_Leu-3,T-cell surface glycoprotein CD4,W3_25 antigen 96T
E1283h ELISA kit Adenocarcinoma-associated antigen,Cell surface glycoprotein Trop-1,EGP,EGP314,EPCAM,Ep-CAM,Epithelial cell adhesion molecule,Epithelial cell surface antigen,Epithelial glycoprotein,Epitheli 96T
EIAAB06400 Cd8b,Cd8b1,Ly-3,Lymphocyte antigen 3,Lyt3,Lyt-3,Mouse,Mus musculus,T-cell membrane glycoprotein Ly-3,T-cell surface glycoprotein CD8 beta chain,T-cell surface glycoprotein Lyt-3
E1283h ELISA Adenocarcinoma-associated antigen,Cell surface glycoprotein Trop-1,EGP,EGP314,EPCAM,Ep-CAM,Epithelial cell adhesion molecule,Epithelial cell surface antigen,Epithelial glycoprotein,Epithelial gl 96T
U1283h CLIA Adenocarcinoma-associated antigen,Cell surface glycoprotein Trop-1,EGP,EGP314,EPCAM,Ep-CAM,Epithelial cell adhesion molecule,Epithelial cell surface antigen,Epithelial glycoprotein,Epithelial gly 96T
E1670h ELISA kit Cell surface glycoprotein MUC18,Cell surface glycoprotein P1H12,Homo sapiens,Human,MCAM,Melanoma cell adhesion molecule,Melanoma-associated antigen A32,Melanoma-associated antigen MUC18,MUC 96T
EIAAB06281 CD1A,Homo sapiens,hTa1 thymocyte antigen,Human,T-cell surface antigen T6_Leu-6,T-cell surface glycoprotein CD1a
E1576m ELISA kit Cd2,LFA-2,LFA-3 receptor,Ly-37,Ly-37,Lymphocyte antigen 37,Mouse,Mus musculus,T-cell surface antigen CD2,T-cell surface antigen T11_Leu-5 96T
U1576m CLIA Cd2,LFA-2,LFA-3 receptor,Ly-37,Ly-37,Lymphocyte antigen 37,Mouse,Mus musculus,T-cell surface antigen CD2,T-cell surface antigen T11_Leu-5 96T
E1576m ELISA Cd2,LFA-2,LFA-3 receptor,Ly-37,Ly-37,Lymphocyte antigen 37,Mouse,Mus musculus,T-cell surface antigen CD2,T-cell surface antigen T11_Leu-5 96T
E1670h ELISA Cell surface glycoprotein MUC18,Cell surface glycoprotein P1H12,Homo sapiens,Human,MCAM,Melanoma cell adhesion molecule,Melanoma-associated antigen A32,Melanoma-associated antigen MUC18,MUC18,S- 96T
U1670h CLIA Cell surface glycoprotein MUC18,Cell surface glycoprotein P1H12,Homo sapiens,Human,MCAM,Melanoma cell adhesion molecule,Melanoma-associated antigen A32,Melanoma-associated antigen MUC18,MUC18,S-e 96T
E1576r ELISA kit Cd2,LFA-2,LFA-3 receptor,OX-34 antigen,Rat,Rattus norvegicus,T-cell surface antigen CD2,T-cell surface antigen T11_Leu-5 96T
E1576r ELISA Cd2,LFA-2,LFA-3 receptor,OX-34 antigen,Rat,Rattus norvegicus,T-cell surface antigen CD2,T-cell surface antigen T11_Leu-5 96T
U1576r CLIA Cd2,LFA-2,LFA-3 receptor,OX-34 antigen,Rat,Rattus norvegicus,T-cell surface antigen CD2,T-cell surface antigen T11_Leu-5 96T
29-715 The CD8 antigen is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. The CD8 antigen, acting as a coreceptor, a 0.05 mg
EIAAB25056 CD200 cell surface glycoprotein receptor,Cd200r1,Cell surface glycoprotein CD200 receptor 1,Cell surface glycoprotein OX2 receptor 1,Mox2r,OX102 antigen,Ox2r,Rat,Rattus norvegicus
20-783-70379 MOUSE ANTI FELINE CD8 ALPHA_BETA - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.25 mg
20-783-72711 MOUSE ANTI RAT CD8 BETA FITC - T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg
20-783-70209 MOUSE ANTI HUMAN CD8 FITC - T8; T-cell surface glycoprotein Lyt-3; T-cell membrane glycoprotein Ly-3; Lymphocyte antigen 3; CD8b antigen Monoclonal 0.1 mg


 

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