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

Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.94) (Multiple substrate lipid kinase) (MuLK) (Multi-substrate lipid kinase)

 AGK_MOUSE               Reviewed;         421 AA.
Q9ESW4; Q9D087;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 129.
RecName: Full=Acylglycerol kinase, mitochondrial {ECO:0000250|UniProtKB:Q53H12};
EC=2.7.1.107 {ECO:0000269|PubMed:15252046};
EC=2.7.1.94 {ECO:0000269|PubMed:15252046};
AltName: Full=Multiple substrate lipid kinase {ECO:0000303|PubMed:15252046};
Short=MuLK {ECO:0000303|PubMed:15252046};
Short=Multi-substrate lipid kinase {ECO:0000303|PubMed:15252046};
Name=Agk {ECO:0000312|MGI:MGI:1917173};
Synonyms=Mulk {ECO:0000303|PubMed:15252046};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
STRAIN=FVB/N; TISSUE=Carcinoma;
PubMed=15252046; DOI=10.1074/jbc.M405932200;
Waggoner D.W., Johnson L.B., Mann P.C., Morris V., Guastella J.,
Bajjalieh S.M.;
"MuLK, a eukaryotic multi-substrate lipid kinase.";
J. Biol. Chem. 279:38228-38235(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=16269826; DOI=10.1194/jlr.M500321-JLR200;
Van Overloop H., Gijsbers S., Van Veldhoven P.P.;
"Further characterization of mammalian ceramide kinase: substrate
delivery and (stereo)specificity, tissue distribution, and subcellular
localization studies.";
J. Lipid Res. 47:268-283(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Lipid kinase that can phosphorylate both
monoacylglycerol and diacylglycerol to form lysophosphatidic acid
(LPA) and phosphatidic acid (PA), respectively (PubMed:15252046).
Does not phosphorylate sphingosine (PubMed:15252046).
Independently of its lipid kinase activity, acts as a component of
the TIM22 complex (By similarity). The TIM22 complex mediates the
import and insertion of multi-pass transmembrane proteins into the
mitochondrial inner membrane by forming a twin-pore translocase
that uses the membrane potential as the external driving force (By
similarity). In the TIM22 complex, required for the import of a
subset of metabolite carriers into mitochtondria, such as
ANT1/SLC25A4 and SLC25A24, while it is not required for the import
of TIMM23 (By similarity). Overexpression increases the formation
and secretion of LPA, resulting in transactivation of EGFR and
activation of the downstream MAPK signaling pathway, leading to
increased cell growth (By similarity).
{ECO:0000250|UniProtKB:Q53H12, ECO:0000269|PubMed:15252046}.
-!- CATALYTIC ACTIVITY: ATP + acylglycerol = ADP + acyl-sn-glycerol 3-
phosphate. {ECO:0000250|UniProtKB:Q53H12,
ECO:0000269|PubMed:15252046}.
-!- CATALYTIC ACTIVITY: ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-
diacyl-sn-glycerol 3-phosphate. {ECO:0000269|PubMed:15252046}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q53H12};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=45 uM for diacylglycerol {ECO:0000269|PubMed:15252046};
Vmax=159 nmol/min/mg enzyme with dioeoylglycerol as substrate
{ECO:0000269|PubMed:15252046};
-!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
{ECO:0000269|PubMed:15252046}.
-!- SUBUNIT: Component of the TIM22 complex, which core is composed of
TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9,
AGK and TIMM29. {ECO:0000250|UniProtKB:Q53H12}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q53H12}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q53H12}. Mitochondrion intermembrane space
{ECO:0000250|UniProtKB:Q53H12}. Note=Localizes in the
mitochondrion intermembrane space, where it associates with the
inner membrane. It is unclear whether the N-terminal hydrophobic
region forms a transmembrane region or associates with the
membrane without crossing it. {ECO:0000250|UniProtKB:Q53H12}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9ESW4-1; Sequence=Displayed;
Name=2;
IsoId=Q9ESW4-2; Sequence=VSP_020927;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:15252046}.
-!- SIMILARITY: Belongs to the AGK family. {ECO:0000305}.
-!- CAUTION: Was originally (PubMed:15252046) thought to have ceramide
kinase activity. Such activity is however unlikely in vivo.
{ECO:0000305|PubMed:15252046}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY772469; AAV38106.1; -; mRNA.
EMBL; AJ401619; CAC06108.1; -; mRNA.
EMBL; AK011715; BAB27796.1; -; mRNA.
EMBL; AK076224; BAC36260.1; -; mRNA.
EMBL; BC019145; AAH19145.1; -; mRNA.
EMBL; BC093525; AAH93525.1; -; mRNA.
CCDS; CCDS20027.1; -. [Q9ESW4-1]
RefSeq; NP_076027.1; NM_023538.2. [Q9ESW4-1]
UniGene; Mm.32840; -.
ProteinModelPortal; Q9ESW4; -.
BioGrid; 213759; 1.
IntAct; Q9ESW4; 2.
MINT; MINT-4129364; -.
STRING; 10090.ENSMUSP00000031977; -.
SwissLipids; SLP:000000885; -.
iPTMnet; Q9ESW4; -.
PhosphoSitePlus; Q9ESW4; -.
EPD; Q9ESW4; -.
PaxDb; Q9ESW4; -.
PeptideAtlas; Q9ESW4; -.
PRIDE; Q9ESW4; -.
DNASU; 69923; -.
Ensembl; ENSMUST00000031977; ENSMUSP00000031977; ENSMUSG00000029916. [Q9ESW4-1]
GeneID; 69923; -.
KEGG; mmu:69923; -.
UCSC; uc009bmm.2; mouse. [Q9ESW4-2]
UCSC; uc009bmn.2; mouse. [Q9ESW4-1]
CTD; 55750; -.
MGI; MGI:1917173; Agk.
eggNOG; KOG4435; Eukaryota.
eggNOG; COG1597; LUCA.
GeneTree; ENSGT00690000101761; -.
HOGENOM; HOG000252977; -.
HOVERGEN; HBG080751; -.
InParanoid; Q9ESW4; -.
KO; K09881; -.
OMA; TKAAHFF; -.
OrthoDB; EOG091G06YD; -.
PhylomeDB; Q9ESW4; -.
TreeFam; TF320485; -.
Reactome; R-MMU-1483206; Glycerophospholipid biosynthesis.
SABIO-RK; Q9ESW4; -.
UniPathway; UPA00230; -.
ChiTaRS; Agk; mouse.
PRO; PR:Q9ESW4; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029916; -.
CleanEx; MM_AGK; -.
ExpressionAtlas; Q9ESW4; baseline and differential.
Genevisible; Q9ESW4; MM.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0042721; C:mitochondrial inner membrane protein insertion complex; ISS:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0047620; F:acylglycerol kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0001729; F:ceramide kinase activity; IDA:MGI.
GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
GO; GO:0001727; F:lipid kinase activity; IDA:MGI.
GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0046834; P:lipid phosphorylation; IDA:MGI.
GO; GO:0045039; P:protein import into mitochondrial inner membrane; ISS:UniProtKB.
Gene3D; 3.40.50.10330; -; 1.
InterPro; IPR017438; ATP-NAD_kinase_N.
InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
Pfam; PF00781; DAGK_cat; 1.
SMART; SM00046; DAGKc; 1.
SUPFAM; SSF111331; SSF111331; 2.
PROSITE; PS50146; DAGK; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Kinase;
Membrane; Mitochondrion; Mitochondrion inner membrane;
Nucleotide-binding; Reference proteome; Transferase.
CHAIN 1 421 Acylglycerol kinase, mitochondrial.
/FTId=PRO_0000252381.
DOMAIN 58 199 DAGKc. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
REGION 15 31 Hydrophobic.
{ECO:0000250|UniProtKB:Q53H12}.
VAR_SEQ 174 421 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020927.
SEQUENCE 421 AA; 46976 MW; DBBC48C9EB3206FD CRC64;
MTAFFKTLRN HWKKTTAGLC LLTWGGHWLY GKHCDNLLRR AACQEAQVFG NQLIPPNAQV
KKATVFLNPA ACKGKARTLF EKNAAPILHL SGMDVTVVKT DYEGQAKKLL ELMESTDVII
VAGGDGTLQE VVTGVLRRTD EATFSKIPIG FIPLGQTSSL SHTLFAESGN KVQHITDATL
AIVKGETVPL DVLQIKGEKE QPVYAMTGLR WGSFRDAGVK VSKYWYLGPL KTKAAHFFST
LQEWPQTHQA SISYTGPRER PPIEPEETPP RPSLYRRILR RLASFWAQPQ DASSREVSPE
VWKDVQLSTI ELSITTRNTQ LDLMSKEDFM NICIEPDTVS KGDFIIIGSK KVRDPGLRAA
GTECLQASHC TLVLPEGTEG SFSIDSEEYE AMPVEVKLLP RKLRFFCDPR KREQMLPSTS
Q


Related products :

Catalog number Product name Quantity
40560 PI-3 Kinase Lipid Substrate 1 mg
GWB-BC2775 PI-3 Kinase Lipid Substrate
40560 PI_3 Kinase Lipid Substrate 1 mg
EIAAB06878 Acylsphingosine kinase,Ceramide kinase,CERK,hCERK,Homo sapiens,Human,KIAA1646,Lipid kinase 4,LK4
18-783-75546 RABBIT ANTI HUMAN CERAMIDE KINASE (N-TERMINAL) - CERK; EC 2.7.1.138; Acylsphingosine kinase; hCERK; Lipid kinase 4; LK4 Polyclonal 0.05 mg
EIAAB44219 Homo sapiens,Human,STK22 substrate 1,STK22S1,Testis-specific kinase substrate,Testis-specific serine kinase substrate,TSKS,TSKS1
EIAAB44221 Rat,Rattus norvegicus,STK22 substrate 1,Stk22s1,Testis-specific kinase substrate,Testis-specific serine kinase substrate,Tsks
EIAAB44220 Mouse,Mus musculus,STK22 substrate 1,Stk22s1,Testis-specific kinase substrate,Testis-specific serine kinase substrate,Tsks
29-689 PLIN coats lipid storage droplets in adipocytes, thereby protecting them until they can be broken down by hormone-sensitive lipase. The protein is the major cAMP-dependent protein kinase substrate in 0.1 mg
18-662-20067 Myristoylated alanine-rich C-kinase substrate - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.1 ml
EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
201-20-4010 PACSIN3{protein kinase C and casein kinase substrate in neurons 3}rabbit.pAb 0.2ml
201-20-4009 PACSIN2{protein kinase C and casein kinase substrate in neurons 2}rabbit.pAb 0.2ml
201-20-4008 PACSIN1{protein kinase C and casein kinase substrate in neurons 1}rabbit.pAb 0.2ml
PACSIN3 PACSIN1 Gene protein kinase C and casein kinase substrate in neurons 1
PADI1 PACSIN2 Gene protein kinase C and casein kinase substrate in neurons 2
PADI2 PACSIN3 Gene protein kinase C and casein kinase substrate in neurons 3
18-003-44331 Protein kinase C and casein kinase substrate in neurons 1 - N_A Polyclonal 0.1 mg Protein A
NUDCD1 NUCKS1 Gene nuclear casein kinase and cyclin-dependent kinase substrate 1


 

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