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

Carbohydrate sulfotransferase 15 (EC 2.8.2.33) (B-cell RAG-associated gene protein) (N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase) (GalNAc4S-6ST)

 CHSTF_MOUSE             Reviewed;         561 AA.
Q91XQ5; Q80TW4; Q8BLQ5; Q9D2N6;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 121.
RecName: Full=Carbohydrate sulfotransferase 15;
EC=2.8.2.33;
AltName: Full=B-cell RAG-associated gene protein;
AltName: Full=N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
Short=GalNAc4S-6ST;
Name=Chst15; Synonyms=Brag, Galnac4s6st, Kiaa0598;
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].
PubMed=9754571;
DOI=10.1002/(SICI)1521-4141(199809)28:09<2839::AID-IMMU2839>3.0.CO;2-6;
Verkoczy L.K., Marsden P.A., Berinstein N.L.;
"hBRAG, a novel B cell lineage cDNA encoding a type II transmembrane
glycoprotein potentially involved in the regulation of recombination
activating gene 1 (RAG1).";
Eur. J. Immunol. 28:2839-2853(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Ohtake S., Morisaki T., Kondo S., Matsumura K., Kimata K., Habuchi O.;
"Characterization of GalNAc 4-sulfate 6-O-sulfotransferase expressed
in bone marrow derived mast cells synthesizing chondroitin sulfate
E.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain cortex, Cerebellum, Skin, and Urinary bladder;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
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).
-!- FUNCTION: Sulfotransferase that transfers sulfate from 3'-
phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl
group of the GalNAc 4-sulfate residue of chondroitin sulfate A and
forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4))
repeating units. It also transfers sulfate to a unique non-
reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4),
to yield a highly sulfated structure similar to the structure
found in thrombomodulin chondroitin sulfate. May also act as a B-
cell receptor involved in BCR ligation-mediated early activation
that mediate regulatory signals key to B-cell development and/or
regulation of B-cell-specific RAG expression; however such results
are unclear in vivo (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 3-phospho-5-adenylyl sulfate + [dermatan]-4-O-
sulfo-N-acetylgalactosamine = adenosine 3',5'-bisphosphate +
[dermatan]-4,6-di-O-sulfo-N-acetyl-D-galactosamine.
-!- CATALYTIC ACTIVITY: 3-phospho-5-adenylyl sulfate + [chondroitin]-
4-O-sulfo-N-acetylgalactosamine = adenosine 3',5'-bisphosphate +
[chondroitin]-4,6-di-O-sulfo-N-acetyl-D-galactosamine.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
-!- COFACTOR:
Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by phenyl beta-GalNAc(4,6-SO(4)).
-!- SUBUNIT: Homodimer; disulfide-linked (Potential). The relevance of
homodimerization is however unsure. May interact with
phosphorylated proteins in resting B-cells, including HCK (By
similarity). {ECO:0000250, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}. Note=A small
fraction may also be present at the cell surface, where it acts as
a B-cell receptor.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC65606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF320786; AAK69604.1; -; mRNA.
EMBL; AB187269; BAD89559.1; -; mRNA.
EMBL; AK122324; BAC65606.1; ALT_INIT; mRNA.
EMBL; AK019474; BAB31743.1; -; mRNA.
EMBL; AK035637; BAC29133.1; -; mRNA.
EMBL; AK043803; BAC31658.1; -; mRNA.
EMBL; AK082318; BAC38463.1; -; mRNA.
EMBL; AK083614; BAC38968.1; -; mRNA.
EMBL; BC031443; AAH31443.1; -; mRNA.
CCDS; CCDS21922.1; -.
RefSeq; NP_084211.2; NM_029935.5.
RefSeq; XP_006508395.1; XM_006508332.1.
RefSeq; XP_006508396.1; XM_006508333.3.
RefSeq; XP_017167875.1; XM_017312386.1.
UniGene; Mm.213582; -.
ProteinModelPortal; Q91XQ5; -.
STRING; 10090.ENSMUSP00000076682; -.
iPTMnet; Q91XQ5; -.
PhosphoSitePlus; Q91XQ5; -.
MaxQB; Q91XQ5; -.
PaxDb; Q91XQ5; -.
PRIDE; Q91XQ5; -.
Ensembl; ENSMUST00000077472; ENSMUSP00000076682; ENSMUSG00000030930.
Ensembl; ENSMUST00000080215; ENSMUSP00000079105; ENSMUSG00000030930.
GeneID; 77590; -.
KEGG; mmu:77590; -.
UCSC; uc009kbx.1; mouse.
CTD; 51363; -.
MGI; MGI:1924840; Chst15.
eggNOG; ENOG410IISS; Eukaryota.
eggNOG; ENOG410XSMU; LUCA.
GeneTree; ENSGT00390000004719; -.
HOGENOM; HOG000154435; -.
InParanoid; Q91XQ5; -.
KO; K08106; -.
OMA; HASNVKY; -.
OrthoDB; EOG091G039B; -.
PhylomeDB; Q91XQ5; -.
TreeFam; TF333516; -.
BRENDA; 2.8.2.33; 3474.
Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
PRO; PR:Q91XQ5; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030930; -.
CleanEx; MM_4631426J05RIK; -.
Genevisible; Q91XQ5; MM.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISS:UniProtKB.
GO; GO:0050659; F:N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity; ISS:UniProtKB.
GO; GO:0019319; P:hexose biosynthetic process; ISS:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
SUPFAM; SSF52540; SSF52540; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Golgi apparatus;
Membrane; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 561 Carbohydrate sulfotransferase 15.
/FTId=PRO_0000225624.
TOPO_DOM 1 80 Cytoplasmic. {ECO:0000255}.
TRANSMEM 81 101 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 102 561 Lumenal. {ECO:0000255}.
NP_BIND 263 267 PAPS. {ECO:0000250}.
BINDING 392 392 PAPS. {ECO:0000250}.
BINDING 400 400 PAPS. {ECO:0000250}.
CARBOHYD 364 364 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 115 115 G -> S (in Ref. 4; BAB31743).
{ECO:0000305}.
CONFLICT 535 535 I -> V (in Ref. 4; BAC31658).
{ECO:0000305}.
SEQUENCE 561 AA; 64986 MW; E00ADD0584559278 CRC64;
MRHCINCCVQ LFPEDTHKQQ VACQGGPHHS HQACPTCKGE NKILFRVDSK QMNLLAVLEV
RTEGNENWGG FLRFRKGKRC SLVFGLIIMT LVMASYILSG AHQELLISSP FHYGGFPSNP
SVMDGENPSD VKEHHYQPSV NNISYVKDYP SIKLIIDSIA ARIEFTTRQL PDLQDLKRQE
LHMFSVIPSK FLPTSKSPCW YEEFSGRNTT DPYLTNSYVL YSKRFRSTFD ALRKVFWGHL
SHVQGKHFRL RCLPHFYIIG QPKCGTTDLY DRLRLHPEVK FSAIKEPHWW TRKRFGIVRL
RDGLRDRYPV EDYLDLFDLA AHQIHQGLQA ASAEQPSKMN KIIIGEASAS TMWDNNAWTF
FYDNSTDGEP PFLTQDFIHA FQPEAKLIVM LRDPVERLYS DYLYFASSNK SADDFHEKVT
EALQLFENCM LDYSLRACVY NNTLNNAMPV RLQVGLYAVY LLDWLTVFSK EQFLILRLED
HASNVKYTMH KVFQFLNLGP LSEKQEALMT KSPASNTRRP EDRSLGPMWP ITQKILREFY
GPFNTRLAQV LDDEAFAWKT T


Related products :

Catalog number Product name Quantity
EIAAB07301 B-cell RAG-associated gene protein,Brag,Carbohydrate sulfotransferase 15,Chst15,Galnac4s6st,GalNAc4S-6ST,Kiaa0598,Mouse,Mus musculus,N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
EIAAB07302 B-cell RAG-associated gene protein,BRAG,Carbohydrate sulfotransferase 15,CHST15,GALNAC4S6ST,GalNAc4S-6ST,hBRAG,Homo sapiens,Human,KIAA0598,N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
EIAAB07303 Carbohydrate sulfotransferase 15,Chst15,Galnac4s6st,GalNAc4S-6ST,N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase,Rat,Rattus norvegicus
CHST3 CHST15 Gene carbohydrate (N-acetylgalactosamine 4-sulfate 6-O) sulfotransferase 15
EIAAB07287 Carbohydrate sulfotransferase 9,CHST9,GalNAc-4-O-sulfotransferase 2,GalNAc-4-ST2,GalNAc4ST-2,Homo sapiens,Human,N-acetylgalactosamine-4-O-sulfotransferase 2,UNQ2549_PRO6175
EIAAB07286 Carbohydrate sulfotransferase 8,CHST8,GalNAc-4-O-sulfotransferase 1,GalNAc-4-ST1,GalNAc4ST-1,Homo sapiens,Human,N-acetylgalactosamine-4-O-sulfotransferase 1
EIAAB07288 Carbohydrate sulfotransferase 9,Chst9,GalNAc-4-O-sulfotransferase 2,GalNAc-4-ST2,GalNAc4ST-2,Mouse,Mus musculus,N-acetylgalactosamine-4-O-sulfotransferase 2
EIAAB07285 Carbohydrate sulfotransferase 8,Chst8,GalNAc-4-O-sulfotransferase 1,GalNAc-4-ST1,GalNAc4ST-1,Mouse,Mus musculus,N-acetylgalactosamine-4-O-sulfotransferase 1
EIAAB07269 Carbohydrate sulfotransferase 1,Chst1,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 1,GST-1,Keratan sulfate Gal-6 sulfotransferase,KS6ST,KSGal6ST,KSST,Rat,Rattus norvegicus
EIAAB07270 Carbohydrate sulfotransferase 1,CHST1,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 1,GST-1,Homo sapiens,Human,Keratan sulfate Gal-6 sulfotransferase,KS6ST,KSGal6ST,KSST
EIAAB07268 Carbohydrate sulfotransferase 1,Chst1,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 1,Gst1,GST-1,Keratan sulfate Gal-6 sulfotransferase,KS6ST,KSGal6ST,KSST,Mouse,Mus musculus
CHSY3 CHST9 Gene carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 9
CHSY1 CHST8 Gene carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 8
CHST2 CHST14 Gene carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14
EIAAB07274 C6ST-1,Carbohydrate sulfotransferase 3,Chondroitin 6-O-sulfotransferase 1,Chondroitin 6-sulfotransferase,CHST3,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 0,GST-0,Homo sapie
EIAAB07297 C4ST2,C4ST-2,Carbohydrate sulfotransferase 12,Chondroitin 4-O-sulfotransferase 2,Chondroitin 4-sulfotransferase 2,CHST12,Homo sapiens,Human,Sulfotransferase Hlo,UNQ500_PRO1017
26-191 GALNAC4S-6ST is a sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms 0.05 mg
18-003-44263 Carbohydrate sulfotransferase 7 - EC 2.8.2.17; EC 2.8.2.-; Chondroitin 6-sulfotransferase 2; C6ST-2; N-acetylglucosamine 6-O-sulfotransferase 1; GlcNAc6ST-4; Galactose_N-acetylglucosamine_N-acetylgluc 0.1 mg Protein A
EIAAB07276 C6ST-1,Carbohydrate sulfotransferase 3,Chondroitin 6-O-sulfotransferase 1,Chst3,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 0,GST-0,Rat,Rattus norvegicus
EIAAB07284 C6ST-2,Carbohydrate sulfotransferase 7,Chondroitin 6-sulfotransferase 2,CHST7,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 5,GlcNAc6ST-4,Gn6st-4,GST-5,Homo sapiens,Human,N-ac
EIAAB07283 C6ST-2,Carbohydrate sulfotransferase 7,Chondroitin 6-sulfotransferase 2,Chst7,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 5,GlcNAc6ST-4,Gn6st-4,Gst5,GST-5,mC6ST-2,Mouse,Mus
CHST11 CHST1 Gene carbohydrate (keratan sulfate Gal-6) sulfotransferase 1
EIAAB07275 C6st,C6ST-1,Carbohydrate sulfotransferase 3,Chondroitin 6-O-sulfotransferase 1,Chst3,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 0,Gst0,GST-0,Mouse,Mus musculus
EIAAB07282 C6ST-2,Carbohydrate sulfotransferase 7,Chondroitin 6-sulfotransferase 2,Chst7,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 5,GlcNAc6ST-4,Gn6st-4,GST-5,N-acetylglucosamine 6-O
EIAAB07298 C4ST3,C4ST-3,Carbohydrate sulfotransferase 13,Chondroitin 4-O-sulfotransferase 3,Chondroitin 4-sulfotransferase 3,CHST13,Homo sapiens,Human


 

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