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

Lysosome membrane protein 2 (85 kDa lysosomal membrane sialoglycoprotein) (LGP85) (Lysosome membrane protein II) (LIMP II) (Scavenger receptor class B member 2)

 SCRB2_MOUSE             Reviewed;         478 AA.
O35114; Q3UNF8;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 129.
RecName: Full=Lysosome membrane protein 2;
AltName: Full=85 kDa lysosomal membrane sialoglycoprotein;
Short=LGP85;
AltName: Full=Lysosome membrane protein II;
Short=LIMP II;
AltName: Full=Scavenger receptor class B member 2;
Name=Scarb2;
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], CHARACTERIZATION, AND SUBCELLULAR
LOCATION.
TISSUE=Liver;
PubMed=9399579; DOI=10.1093/oxfordjournals.jbchem.a021820;
Tabuchi N., Akasaki K., Sasaki T., Kanda N., Tsuji H.;
"Identification and characterization of a major lysosomal membrane
glycoprotein, LGP85/LIMP II in mouse liver.";
J. Biochem. 122:756-763(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver, and Spinal cord;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=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).
[4]
PROTEIN SEQUENCE OF 276-294 AND 361-378, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
FUNCTION, AND INTERACTION WITH GBA.
PubMed=18022370; DOI=10.1016/j.cell.2007.10.018;
Reczek D., Schwake M., Schroder J., Hughes H., Blanz J., Jin X.,
Brondyk W., Van Patten S., Edmunds T., Saftig P.;
"LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent
targeting of beta-glucocerebrosidase.";
Cell 131:770-783(2007).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
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).
[8]
FUNCTION, INTERACTION WITH GBA, SUBCELLULAR LOCATION, REGION, AND
MUTAGENESIS OF ASN-45; ASN-68; ASN-105; ASN-122; LEU-155; ILE-156;
MET-159; LEU-160; ALA-162; TYR-163; LYS-166; ILE-184; LEU-187;
PHE-191; ASN-206; ASN-224; ASN-249; ASN-304; ASN-325; ASP-400; ASN-412
AND ASN-430.
PubMed=24162852; DOI=10.1038/nature12684;
Neculai D., Schwake M., Ravichandran M., Zunke F., Collins R.F.,
Peters J., Neculai M., Plumb J., Loppnau P., Pizarro J.C., Seitova A.,
Trimble W.S., Saftig P., Grinstein S., Dhe-Paganon S.;
"Structure of LIMP-2 provides functional insights with implications
for SR-BI and CD36.";
Nature 504:172-176(2013).
-!- FUNCTION: Acts as a lysosomal receptor for glucosylceramidase
(GBA) targeting. {ECO:0000269|PubMed:18022370,
ECO:0000269|PubMed:24162852}.
-!- SUBUNIT: Interacts with GBA. {ECO:0000269|PubMed:18022370,
ECO:0000269|PubMed:24162852}.
-!- SUBCELLULAR LOCATION: Lysosome membrane
{ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}; Multi-
pass membrane protein {ECO:0000269|PubMed:24162852,
ECO:0000269|PubMed:9399579}.
-!- TISSUE SPECIFICITY: Detected in the extracts of brain, heart,
lung, liver and kidney.
-!- PTM: Acylated by palmitic acid group(s). {ECO:0000250}.
-!- PTM: Heavily glycosylated. {ECO:0000269|PubMed:19349973}.
-!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB008553; BAA23372.1; -; mRNA.
EMBL; AK011123; BAB27416.1; -; mRNA.
EMBL; AK083038; BAC38740.1; -; mRNA.
EMBL; AK144235; BAE25789.1; -; mRNA.
EMBL; BC029073; AAH29073.1; -; mRNA.
CCDS; CCDS19431.1; -.
PIR; JC5670; JC5670.
RefSeq; NP_031670.1; NM_007644.4.
UniGene; Mm.297964; -.
ProteinModelPortal; O35114; -.
SMR; O35114; -.
IntAct; O35114; 6.
MINT; O35114; -.
STRING; 10090.ENSMUSP00000031377; -.
TCDB; 9.B.39.1.9; the long chain fatty acid translocase (lcfat) family.
iPTMnet; O35114; -.
PhosphoSitePlus; O35114; -.
SwissPalm; O35114; -.
EPD; O35114; -.
MaxQB; O35114; -.
PaxDb; O35114; -.
PeptideAtlas; O35114; -.
PRIDE; O35114; -.
Ensembl; ENSMUST00000031377; ENSMUSP00000031377; ENSMUSG00000029426.
GeneID; 12492; -.
KEGG; mmu:12492; -.
UCSC; uc008ydm.1; mouse.
CTD; 950; -.
MGI; MGI:1196458; Scarb2.
eggNOG; KOG3776; Eukaryota.
eggNOG; ENOG410XS17; LUCA.
GeneTree; ENSGT00530000062927; -.
HOGENOM; HOG000252951; -.
HOVERGEN; HBG106707; -.
InParanoid; O35114; -.
KO; K12384; -.
OMA; KCNMING; -.
OrthoDB; EOG091G0CH9; -.
PhylomeDB; O35114; -.
TreeFam; TF317925; -.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
PRO; PR:O35114; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029426; -.
CleanEx; MM_SCARB2; -.
Genevisible; O35114; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043202; C:lysosomal lumen; IDA:BHF-UCL.
GO; GO:0005765; C:lysosomal membrane; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0001508; P:action potential; IMP:ARUK-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0006622; P:protein targeting to lysosome; IMP:BHF-UCL.
GO; GO:1905123; P:regulation of glucosylceramidase activity; IMP:ParkinsonsUK-UCL.
InterPro; IPR002159; CD36_fam.
InterPro; IPR005429; LimpII.
PANTHER; PTHR11923; PTHR11923; 1.
Pfam; PF01130; CD36; 1.
PRINTS; PR01609; CD36FAMILY.
PRINTS; PR01611; LIMPII.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Lipoprotein; Lysosome; Membrane; Palmitate; Receptor;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 478 Lysosome membrane protein 2.
/FTId=PRO_0000144156.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 27 Helical. {ECO:0000255}.
TOPO_DOM 28 433 Lumenal. {ECO:0000255}.
TRANSMEM 434 459 Helical. {ECO:0000255}.
TOPO_DOM 460 478 Cytoplasmic. {ECO:0000255}.
REGION 155 191 Important for interaction with GBA.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 274 329 {ECO:0000250}.
DISULFID 312 318 {ECO:0000250}.
MUTAGEN 45 45 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 68 68 N->Q: Loss of glycosylation site. Causes
retention in the endoplasmic reticulum
and abolishes normal location in
lysosomes. {ECO:0000269|PubMed:24162852}.
MUTAGEN 105 105 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 122 122 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 155 155 L->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 156 156 I->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 159 159 M->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 160 160 L->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 162 162 A->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 163 163 Y->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 166 166 K->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 184 184 I->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 187 187 L->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 191 191 F->D: Abolishes interaction with GBA. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 206 206 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 224 224 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 249 249 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 304 304 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 325 325 N->Q: Loss of glycosylation site. Causes
retention in the endoplasmic reticulum
and abolishes normal location in
lysosomes. {ECO:0000269|PubMed:24162852}.
MUTAGEN 400 400 D->K: Slightly increased GBA binding. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 412 412 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
MUTAGEN 430 430 N->Q: Loss of glycosylation site. No
effect on normal location in lysosomes.
{ECO:0000269|PubMed:24162852}.
SEQUENCE 478 AA; 54044 MW; 55724B77855470DF CRC64;
MGRCCFYTAG TLSLLLLVTS VTLLVARVFQ KAVDQTIEKN MVLQNGTKVF NSWEKPPLPV
YIQFYFFNVT NPEEILQGEI PLLEEVGPYT YRELRNKANI QFGENGTTIS AVTNKAYVFE
RNQSVGDPNV DLIRTINIPL LTVVDLAQLT LLRELIEAML KAYQQKLFVI HTVHELLWGY
KDEILSLVHI FKPDVSPNFG LFYERNGTND GEYVFLTGED NYLNFSKIVE WNGKTSLDWW
TTDTCNMING TDGDSFHPLI SKDEVLYLFP SDLCRSVHIT FSSFENVEGL PAFRYKVPAE
ILANTSENAG FCIPEGNCMD SGVLNISICK NGAPIIMSFP HFYQADEKFV SAIKGMHPNK
EEHESFVDIN PLTGIILRGA KRFQINTYVR KLDDFVETGD IRTMVFPVMY LNESVLIDKE
TANQLKSVIN TTLVVTNIPY IIMALGVFFG LVFTWLACRG QGSMDEGTAD ERAPLIRT


Related products :

Catalog number Product name Quantity
EIAAB37666 85 kDa lysosomal membrane sialoglycoprotein,LGP85,LIMP II,Lysosome membrane protein 2,Lysosome membrane protein II,Mouse,Mus musculus,Scarb2,Scavenger receptor class B member 2
EIAAB37664 85 kDa lysosomal membrane sialoglycoprotein,CD36 antigen-like 2,CD36L2,Homo sapiens,Human,LGP85,LIMP II,LIMPII,Lysosome membrane protein 2,Lysosome membrane protein II,SCARB2,Scavenger receptor class
EIAAB37665 85 kDa lysosomal membrane sialoglycoprotein,CD36 antigen-like 2,Cd36l2,LGP85,LIMP II,Limpii,Lysosome membrane protein 2,Lysosome membrane protein II,Rat,Rattus norvegicus,Scarb2,Scavenger receptor cla
E1464m ELISA kit CD107 antigen-like family member B,Lamp2,LAMP-2,Lamp-2,LGP-B,Lysosomal membrane glycoprotein type B,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2,Mouse, 96T
U1464m CLIA CD107 antigen-like family member B,Lamp2,LAMP-2,Lamp-2,LGP-B,Lysosomal membrane glycoprotein type B,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2,Mouse,Mus mu 96T
E1464m ELISA CD107 antigen-like family member B,Lamp2,LAMP-2,Lamp-2,LGP-B,Lysosomal membrane glycoprotein type B,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2,Mouse,Mus m 96T
U1464r CLIA CD107 antigen-like family member B,Lamp2,LAMP-2,Lamp-2,LGP-110,LGP-96,LGP-B,Lysosomal membrane glycoprotein type B,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 96T
E1464r ELISA CD107 antigen-like family member B,Lamp2,LAMP-2,Lamp-2,LGP-110,LGP-96,LGP-B,Lysosomal membrane glycoprotein type B,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protei 96T
E1464r ELISA kit CD107 antigen-like family member B,Lamp2,LAMP-2,Lamp-2,LGP-110,LGP-96,LGP-B,Lysosomal membrane glycoprotein type B,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane p 96T
E1464h ELISA kit CD107 antigen-like family member B,Homo sapiens,Human,LAMP2,LAMP-2,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2 96T
U1464h CLIA CD107 antigen-like family member B,Homo sapiens,Human,LAMP2,LAMP-2,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2 96T
E1464h ELISA CD107 antigen-like family member B,Homo sapiens,Human,LAMP2,LAMP-2,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2 96T
E1464c ELISA kit Chicken,Gallus gallus,LAMP2,LAMP-2,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2 96T
U1464c CLIA Chicken,Gallus gallus,LAMP2,LAMP-2,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2 96T
E1464c ELISA Chicken,Gallus gallus,LAMP2,LAMP-2,Lysosome-associated membrane glycoprotein 2,Lysosome-associated membrane protein 2 96T
PC-541 LAMP_1 (Lysosome Associated Membrane Protein 1) 100 ug
PC-542 LAMP_2 (Lysosome Associated Membrane Protein 2) 100 ug
PC-542 LAMP_2 (Lysosome Associated Membrane Protein 2) Poly 100 ug
PC-541 LAMP_1 (Lysosome Associated Membrane Protein 1) Poly 100 ug
E1196r Rat ELISA Kit FOR Lysosome membrane protein 2 96T
PC-541 LAMP_1 (Lysosome Associated Membrane Protein 1) Clone Poly 100 ug
K88104R Lysosome Associated Membrane Protein 2 (LAMP-2)Rabbit Aff.Pur. 100ug
PC-542 LAMP_2 (Lysosome Associated Membrane Protein 2) Clone Poly 100 ug
SCRB2_HUMAN Human ELISA Kit FOR Lysosome membrane protein 2 96T
CSB-EL020768RA Rat Lysosome membrane protein 2(SCARB2) ELISA kit 96T


 

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