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

Ephrin type-A receptor 2 (EC 2.7.10.1)

 EPHA2_MACFA             Reviewed;         976 AA.
Q1KL86;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 1.
22-NOV-2017, entry version 86.
RecName: Full=Ephrin type-A receptor 2;
EC=2.7.10.1;
Flags: Precursor;
Name=EPHA2;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin;
Walsh W.D., Bruckheimer E.M.;
"Macaca fascicularis EPH receptor A2 (EPHA2).";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
membrane-bound ephrin-A family ligands residing on adjacent cells,
leading to contact-dependent bidirectional signaling into
neighboring cells. The signaling pathway downstream of the
receptor is referred to as forward signaling while the signaling
pathway downstream of the ephrin ligand is referred to as reverse
signaling. Activated by the ligand ephrin-A1/EFNA1 regulates
migration, integrin-mediated adhesion, proliferation and
differentiation of cells. Regulates cell adhesion and
differentiation through DSG1/desmoglein-1 and inhibition of the
ERK1/ERK2 signaling pathway. May also participate in UV radiation-
induced apoptosis and have a ligand-independent stimulatory effect
on chemotactic cell migration. During development, may function in
distinctive aspects of pattern formation and subsequently in
development of several fetal tissues. Involved for instance in
angiogenesis, in early hindbrain development and epithelial
proliferation and branching morphogenesis during mammary gland
development. Engaged by the ligand ephrin-A5/EFNA5 may regulate
lens fiber cells shape and interactions and be important for lens
transparency development and maintenance. With ephrin-A2/EFNA2 may
play a role in bone remodeling through regulation of
osteoclastogenesis and osteoblastogenesis (By similarity).
{ECO:0000250|UniProtKB:P29317}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Homodimer. Interacts with SLA. Interacts (phosphorylated
form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2
or PIK3R3); critical for the EFNA1-induced activation of RAC1
which stimulates cell migration. Interacts with INPPL1; regulates
activated EPHA2 endocytosis and degradation. Interacts
(inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-
activated form) with PTPN11; regulates integrin-mediated adhesion.
Interacts with ARHGEF16, DOCK4 and ELMO2; mediates ligand-
independent activation of RAC1 which stimulates cell migration.
Interacts with CLDN4; phosphorylates CLDN4 and may regulate tight
junctions. Interacts with ACP1. Interacts with ANKS1A. Interacts
with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in
cell migration and adhesion (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, lamellipodium membrane
{ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane
protein {ECO:0000255}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:P29317}. Note=Present at regions of cell-
cell contacts but also at the leading edge of migrating cells.
Relocates from the plasma membrane to the cytoplasmic and
perinuclear regions in cancer cells.
{ECO:0000250|UniProtKB:P29317}.
-!- PTM: Autophosphorylates. Phosphorylated on tyrosine upon binding
and activation by EFNA1. Phosphorylated residues Tyr-588 and Tyr-
594 are required for binding VAV2 and VAV3 while phosphorylated
residues Tyr-735 and Tyr-930 are required for binding PI3-kinase
p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated
residues are critical for recruitment of VAV2 and VAV3 and PI3-
kinase p85 subunit which transduce downstream signaling to
activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-
930 by PTPRF prevents the interaction of EPHA2 with NCK1.
Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation
which targets EPHA2 to the cell leading edge and stimulates cell
migration. Phosphorylation by PKB is inhibited by EFNA1-activated
EPHA2 which regulates PKB activity via a reciprocal regulatory
loop. Phosphorylated at Ser-897 in response to TNF by RPS6KA1 and
RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration.
Phosphorylated at Ser-897 by PKA; blocks cell retraction induced
by EPHA2 kinase activity. Dephosphorylated by ACP1.
{ECO:0000250|UniProtKB:P29317, ECO:0000250|UniProtKB:Q03145}.
-!- PTM: Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by
the HSP90 chaperone and regulates the receptor stability and
activity through proteasomal degradation. ANKS1A prevents
ubiquitination and degradation (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ478608; ABE96827.1; -; mRNA.
RefSeq; NP_001306345.1; NM_001319416.1.
UniGene; Mfa.8132; -.
ProteinModelPortal; Q1KL86; -.
SMR; Q1KL86; -.
PRIDE; Q1KL86; -.
GeneID; 102146108; -.
KEGG; mcf:102146108; -.
CTD; 1969; -.
HOVERGEN; HBG062180; -.
KO; K05103; -.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0031256; C:leading edge membrane; ISS:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0046849; P:bone remodeling; ISS:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; ISS:UniProtKB.
GO; GO:0046058; P:cAMP metabolic process; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0048870; P:cell motility; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0070309; P:lens fiber cell morphogenesis; ISS:UniProtKB.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0010591; P:regulation of lamellipodium assembly; ISS:UniProtKB.
GO; GO:0070848; P:response to growth factor; ISS:UniProtKB.
CDD; cd10480; EphR_LBD_A2; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034263; EphA2_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
2: Evidence at transcript level;
Angiogenesis; Apoptosis; ATP-binding; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Differentiation; Disulfide bond;
Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Receptor; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 976 Ephrin type-A receptor 2.
/FTId=PRO_0000260316.
TOPO_DOM 25 537 Extracellular. {ECO:0000255}.
TRANSMEM 538 558 Helical. {ECO:0000255}.
TOPO_DOM 559 976 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 206 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 328 432 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 438 529 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 613 875 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 904 968 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 619 627 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 206 Mediates interaction with CLDN4.
{ECO:0000250}.
REGION 606 906 Mediates interaction with ARHGEF16.
{ECO:0000250}.
REGION 886 976 Negatively regulates interaction with
ARHGEF16. {ECO:0000250}.
MOTIF 974 976 PDZ-binding. {ECO:0000255}.
COMPBIAS 188 325 Cys-rich.
ACT_SITE 739 739 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 646 646 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 575 575 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 579 579 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 588 588 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 594 594 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q03145}.
MOD_RES 628 628 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 647 647 Phosphothreonine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 735 735 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q03145}.
MOD_RES 772 772 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q03145}.
MOD_RES 869 869 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 897 897 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 901 901 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 921 921 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 930 930 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29317}.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 70 188 {ECO:0000250}.
DISULFID 105 115 {ECO:0000250}.
SEQUENCE 976 AA; 108506 MW; 244DD74D78F14EFB CRC64;
MELWAARACF VLLWGCALAP ATAAQGKEVV LLDFAAAGGE LGWLTHPYGK GWDLMQNIMN
DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF TVRDCNSFPG GASSCKETFN
LYYAESDLDY GTNFQKRLFT KIDTIAPDEI TVSSDFEARH VKLNVEERSV GPLTRKGFYL
AFQDIGACVA LLSVRVYYKK CPELLQSLAR FPETIAGSDA PSLATVAGTC VDHAVVPPGG
EEPRMHCAVD GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEVSESPC LECPEHTLPS
PEGATSCECE EGFFRAPQDP MSMPCTRPPS APHYLTAVGM GAKVELRWTP PQDSGGREDI
VYSVTCEQCW PESGECGPCE SSVRYSEPPH GLTRTSVTVS DLEPHMNYTF TVEARNGVSG
LVTSRSFRTA SVSINQTEPP KVRLEGRSTT SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN
SYNVRRTEGF SVTLDDLAPD TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGSLAVIGG
VAVCVVLLLL LAGAGFFIHR RRKNLRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA
VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG TLKTSSGKKE VPVAIKTLKA GYTEKQRVDF
LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEFMENGAL DKFLREKDGE FSVLQLVGML
RGIAAGMKYL ANMNYVHRDL AARNILVNSN LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP
IRWTAPEAIS YRKFTSASDV WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM
DCPSAIYQLM MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG
SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR LPGHQKRIAY
SLLGLKDQVN TVGIPI


Related products :

Catalog number Product name Quantity
LF-PA41414 anti-Ephrin Type A Receptor 2, Rabbit polyclonal to Ephrin Type A Receptor 2, Isotype IgG, Host Rabbit 100 ul
LF-PA40385 anti-Ephrin Type A Receptor 4 (EPHA4) , Rabbit polyclonal to Ephrin Type A Receptor 4 (EPHA4), Isotype IgG, Host Rabbit 50 ug
LF-PA40384 anti-Ephrin Type A Receptor 4 (EPHA4) , Rabbit polyclonal to Ephrin Type A Receptor 4 (EPHA4), Isotype IgG, Host Rabbit 50 ug
EIAAB13101 ELK,Elk,Ephb1,Ephrin type-B receptor 1,Epth2,Rat,Rattus norvegicus,Tyrosine-protein kinase receptor EPH-2
EIAAB13112 Ephb6,Ephrin type-B receptor 6,Rat,Rattus norvegicus,Tyrosine-protein kinase-defective receptor EPH-6
EIAAB13113 EPHB6,Ephrin type-B receptor 6,HEP,Homo sapiens,Human,Tyrosine-protein kinase-defective receptor EPH-6
EIAAB13114 Cekl,Ephb6,Ephrin type-B receptor 6,MEP,Mouse,Mus musculus,Tyrosine-protein kinase-defective receptor EPH-6
X2112P Ephrin Type A Receptor 4 (EPHA4) type: Antigen Immunoaffinity Purified Polyclonal host: Rabbit Isotype: IgG 50
X2247P Ephrin Type A Receptor 4 (EPHA4) type: Antigen Immunoaffinity Purified Polyclonal host: Rabbit Isotype: IgG 50
EH831 Ephrin type-A receptor 4 Elisa Kit 96T
EM640 Ephrin type-B receptor 4 Elisa Kit 96T
EH3007 Ephrin Type A Receptor 10 Elisa Kit 96T
CD11 Ephrin Type-B Receptor 1 EphB1 500
EPHA8_RAT Rat ELISA Kit FOR Ephrin type-A receptor 8 96T
Y105065 Ephrin Type A Receptor 4 (EPHA4) 50ug
EH3006 Ephrin Type A Receptor 1 Elisa Kit 96T
CD11 Ephrin Type-B Receptor 1 EphB1 lmg
EPHA6_RAT Rat ELISA Kit FOR Ephrin type-A receptor 6 96T
C519 Ephrin Type-A Receptor 7 EPHA7 500
orb124612 Ephrin type B receptor 2 antibody (PE) 100 ul
orb130875 Ephrin type B receptor 2 antibody (PE-Cy7) 100 ul
orb123628 Ephrin type B receptor 2 antibody (Cy7) 100 ul
C519 Ephrin Type-A Receptor 7 EPHA7 lmg
orb123136 Ephrin type B receptor 2 antibody (Cy5.5) 100 ul
orb129133 Ephrin type B receptor 2 antibody (PE-Cy3) 100 ul


 

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