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

DNA-(apurinic or apyrimidinic site) lyase 2 (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease 2) (Apurinic-apyrimidinic endonuclease 2) (AP endonuclease 2)

 APEX2_MOUSE             Reviewed;         516 AA.
Q68G58; Q8BJP7; Q8BTR7; Q8BUZ2; Q8BYE9; Q8R018; Q8R328; Q9CS12;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
12-SEP-2018, entry version 110.
RecName: Full=DNA-(apurinic or apyrimidinic site) lyase 2;
EC=3.1.-.-;
EC=4.2.99.18;
AltName: Full=APEX nuclease 2;
AltName: Full=Apurinic-apyrimidinic endonuclease 2;
Short=AP endonuclease 2;
Name=Apex2; Synonyms=Ape2;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION,
INTERACTION WITH PCNA, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=129/Sv, and C57BL/6J; TISSUE=B-cell;
PubMed=12573260; DOI=10.1016/S0888-7543(02)00009-5;
Ide Y., Tsuchimoto D., Tominaga Y., Iwamoto Y., Nakabeppu Y.;
"Characterization of the genomic structure and expression of the mouse
Apex2 gene.";
Genomics 81:47-57(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/2/4/5).
STRAIN=NOD; TISSUE=Adipose tissue, Head, and Thymus;
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] (ISOFORMS 1 AND 3).
STRAIN=FVB/N-3; 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]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=15319281; DOI=10.1182/blood-2004-04-1476;
Ide Y., Tsuchimoto D., Tominaga Y., Nakashima M., Watanabe T.,
Sakumi K., Ohno M., Nakabeppu Y.;
"Growth retardation and dyslymphopoiesis accompanied by G2/M arrest in
APEX2-null mice.";
Blood 104:4097-4103(2004).
[5]
FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=18025127; DOI=10.1084/jem.20071289;
Guikema J.E., Linehan E.K., Tsuchimoto D., Nakabeppu Y., Strauss P.R.,
Stavnezer J., Schrader C.E.;
"APE1- and APE2-dependent DNA breaks in immunoglobulin class switch
recombination.";
J. Exp. Med. 204:3017-3026(2007).
[6]
FUNCTION.
PubMed=19556307; DOI=10.1093/intimm/dxp061;
Sabouri Z., Okazaki I.M., Shinkura R., Begum N., Nagaoka H.,
Tsuchimoto D., Nakabeppu Y., Honjo T.;
"Apex2 is required for efficient somatic hypermutation but not for
class switch recombination of immunoglobulin genes.";
Int. Immunol. 21:947-955(2009).
-!- FUNCTION: Function as a weak apurinic/apyrimidinic (AP)
endodeoxyribonuclease in the DNA base excision repair (BER)
pathway of DNA lesions induced by oxidative and alkylating agents.
Initiates repair of AP sites in DNA by catalyzing hydrolytic
incision of the phosphodiester backbone immediately adjacent to
the damage, generating a single-strand break with 5'-deoxyribose
phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA
3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust
3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is
able to remove mismatched nucleotides preferentially. Shows fairly
strong 3'-phosphodiesterase activity involved in the removal of
3'-damaged termini formed in DNA by oxidative agents. In the
nucleus functions in the PCNA-dependent BER pathway. Required for
somatic hypermutation (SHM) and DNA cleavage step of class switch
recombination (CSR) of immunoglobulin genes. Required for proper
cell cycle progression during proliferation of peripheral
lymphocytes. {ECO:0000269|PubMed:12573260,
ECO:0000269|PubMed:15319281, ECO:0000269|PubMed:18025127,
ECO:0000269|PubMed:19556307}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000255|PROSITE-ProRule:PRU00764}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Probably binds two magnesium or manganese ions per subunit.
{ECO:0000250};
-!- ACTIVITY REGULATION: 3'-5' exonuclease activity is activated by
sodium and manganese. 3'-5' exonuclease and 3'-phosphodiesterase
activities are stimulated in presence of PCNA (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with PCNA. This interaction is increased by
misincorporation of uracil in nuclear DNA (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion
{ECO:0000305}. Note=Together with PCNA, is redistributed in
discrete nuclear foci in presence of oxidative DNA damaging
agents.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q68G58-1; Sequence=Displayed;
Name=2;
IsoId=Q68G58-2; Sequence=VSP_015346;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q68G58-3; Sequence=VSP_015349, VSP_015350;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q68G58-4; Sequence=VSP_015347, VSP_015352;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q68G58-5; Sequence=VSP_015348, VSP_015351;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in lymphocytes, thymocytes and
splenocytes (at protein level). Highly expressed in the thymus and
weakly expressed in the bone marrow, spleen, eye, kidney, lung,
brain and uterus. {ECO:0000269|PubMed:12573260,
ECO:0000269|PubMed:15319281}.
-!- INDUCTION: Up-regulated in both the nucleus and the cytosol of B
cells stimulated to switch. {ECO:0000269|PubMed:18025127}.
-!- DISRUPTION PHENOTYPE: Mice show abnormalities in proliferating
haemopoietic organs, such as dyshematopoiesis, defect in
lymphopoiesis, and delayed S-phase and G2/M-phase arrest.
{ECO:0000269|PubMed:15319281, ECO:0000269|PubMed:18025127}.
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA 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; AB072498; BAB88654.1; -; mRNA.
EMBL; AB085235; BAC11807.1; -; Genomic_DNA.
EMBL; AK021248; BAB32346.1; -; mRNA.
EMBL; AK040145; BAC30522.1; -; mRNA.
EMBL; AK050858; BAC34436.1; -; mRNA.
EMBL; AK080916; BAC38077.1; -; mRNA.
EMBL; AK081677; BAC38287.1; -; mRNA.
EMBL; AK088918; BAC40652.1; -; mRNA.
EMBL; BC026769; AAH26769.1; -; mRNA.
EMBL; BC078633; AAH78633.1; -; mRNA.
CCDS; CCDS30463.1; -. [Q68G58-1]
RefSeq; NP_084219.1; NM_029943.2.
RefSeq; XP_011246180.1; XM_011247878.2. [Q68G58-5]
UniGene; Mm.440275; -.
ProteinModelPortal; Q68G58; -.
SMR; Q68G58; -.
IntAct; Q68G58; 1.
STRING; 10090.ENSMUSP00000026303; -.
iPTMnet; Q68G58; -.
PhosphoSitePlus; Q68G58; -.
PaxDb; Q68G58; -.
PRIDE; Q68G58; -.
Ensembl; ENSMUST00000112725; ENSMUSP00000108345; ENSMUSG00000025269. [Q68G58-5]
Ensembl; ENSMUST00000112727; ENSMUSP00000108347; ENSMUSG00000025269. [Q68G58-4]
GeneID; 77622; -.
KEGG; mmu:77622; -.
UCSC; uc009uoi.1; mouse. [Q68G58-5]
CTD; 27301; -.
MGI; MGI:1924872; Apex2.
eggNOG; KOG1294; Eukaryota.
eggNOG; COG0708; LUCA.
GeneTree; ENSGT00530000063540; -.
HOVERGEN; HBG054715; -.
InParanoid; Q68G58; -.
KO; K10772; -.
PRO; PR:Q68G58; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000025269; Expressed in 166 organ(s), highest expression level in ear.
CleanEx; MM_APEX2; -.
ExpressionAtlas; Q68G58; baseline and differential.
Genevisible; Q68G58; MM.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR004808; AP_endonuc_1.
InterPro; IPR020847; AP_endonuclease_F1_BS.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR010666; Znf_GRF.
PANTHER; PTHR22748; PTHR22748; 1.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF06839; zf-GRF; 1.
SUPFAM; SSF56219; SSF56219; 1.
TIGRFAMs; TIGR00633; xth; 1.
PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Complete proteome; Cytoplasm;
DNA damage; DNA recombination; DNA repair; DNA-binding; Endonuclease;
Exonuclease; Hydrolase; Lyase; Magnesium; Metal-binding;
Mitochondrion; Nuclease; Nucleus; Reference proteome.
CHAIN 1 516 DNA-(apurinic or apyrimidinic site) lyase
2.
/FTId=PRO_0000200015.
REGION 389 396 Required for the colocalization with PCNA
in nuclear foci in presence of oxidative-
induced DNA damaging agents.
{ECO:0000250}.
ACT_SITE 155 155 {ECO:0000250}.
ACT_SITE 196 196 Proton donor/acceptor. {ECO:0000250}.
METAL 8 8 Magnesium 1. {ECO:0000250}.
METAL 47 47 Magnesium 1. {ECO:0000250}.
METAL 196 196 Magnesium 2. {ECO:0000250}.
METAL 198 198 Magnesium 2. {ECO:0000250}.
METAL 302 302 Magnesium 1. {ECO:0000250}.
SITE 198 198 Transition state stabilizer.
{ECO:0000250}.
SITE 276 276 Important for catalytic activity.
{ECO:0000250}.
SITE 303 303 Interaction with DNA substrate.
{ECO:0000250}.
VAR_SEQ 79 79 S -> SECSCPSP (in isoform 2).
{ECO:0000305}.
/FTId=VSP_015346.
VAR_SEQ 213 266 ECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSYRYLHPKQ
QRAFTCWSVVSGA -> LPVAACGHTNLVPEWEAGPVWERT
MREIMEGFCDLLHSVRIFHHHTASLLRPSY (in
isoform 4). {ECO:0000305}.
/FTId=VSP_015347.
VAR_SEQ 213 260 ECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSYRYLHPKQ
QRAFTCW -> LPVAACGHTNLVPEWEAGPVWERTMREIME
VKTRFCSRPLKFTESPCL (in isoform 5).
{ECO:0000305}.
/FTId=VSP_015348.
VAR_SEQ 213 246 ECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSY -> VRF
PLNHRPQFCSVHPASQNWEFGTRGSFFYGKK (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015349.
VAR_SEQ 247 516 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015350.
VAR_SEQ 261 516 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_015351.
VAR_SEQ 267 516 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_015352.
CONFLICT 110 110 G -> S (in Ref. 2; BAC38077).
{ECO:0000305}.
CONFLICT 183 183 A -> P (in Ref. 2; BAB32346).
{ECO:0000305}.
CONFLICT 372 372 C -> F (in Ref. 3; AAH78633).
{ECO:0000305}.
CONFLICT 433 433 V -> M (in Ref. 3; AAH78633).
{ECO:0000305}.
SEQUENCE 516 AA; 57340 MW; ED32A88D9CEABB85 CRC64;
MLRVVSWNIN GIRSPLQGLA CQEPSSCPTA LRRVLDELDA DIVCLQETKV TRDVLTEPLA
IVEGYNSYFS FSRSRSGYSG VATFCKDSAT PVAAEEGLSG VFATLNGDIG CYGNMDEFTQ
EELRVLDSEG RALLTQHKIR TLEGKEKTLT LINVYCPHAD PGKPERLTFK MRFYRLLQMR
AEALLAAGSH VIILGDLNTA HRPIDHCDAS SLECFEEDPG RKWMDGLLSN PGDEAGPHIG
LFMDSYRYLH PKQQRAFTCW SVVSGARHLN YGSRLDYVLG DRALVIDTFQ ASFLLPEVMG
SDHCPVGAVL NVSCVPAKQC PALCTRFLPE FAGTQLKILR FLVPLEQEPV REQQVLQPSH
QIQAQRQPRK ACMHSTRLRK SQGGPKRKQK NLMSYFQPSS SLSQTSGVEL PTLPLVGPLT
TPKTAEEVAT ATVLEEKNKV PESKDEKGER TAFWKSMLSG PSPMPLCGGH REPCVMRTVK
KTGPNFGRQF YMCARPRGPP SDPSSRCNFF LWSRPS


Related products :

Catalog number Product name Quantity
18-003-43958 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43959 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43422 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN; Protein REF-1 Polyclonal 0.1 mg Protein A
GWB-9E866F APEX Nuclease (Apurinic Apyrimidinic Endonuclease) 2 (APEX2) Rabbit anti-Human Polyclonal Antibody
EIAAB26876 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,Mouse,Mus musculus,NEH1,Nei homolog 1,Nei1,Neil1,Nei-like protein 1
EIAAB26879 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Homo sapiens,Human,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26878 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Gm1212,Mouse,Mus musculus,NEH2,Nei homolog 2,Neil2,Nei-like protein 2
EIAAB26880 Bos taurus,Bovine,DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26877 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,FPG1,Homo sapiens,Human,NEH1,Nei homolog 1,NEIL1,Nei-like protein 1
C101 Apurinic-Apyrimidinic Endonuclease 1 APE 500
C101 Apurinic-Apyrimidinic Endonuclease 1 APE lmg
CG78 Human Apurinic-Apyrimidinic Endonuclease 1 APE 50
C101 Human Apurinic-Apyrimidinic Endonuclease 1 APE l0
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE 50 ug
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE 10 ug
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE 1 mg
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE 500 ug
EH2009 DNA-(apurinic or apyrimidinic site) lyase Elisa Kit 96T
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE, Source: E. coli 10μg
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE, Source: E. coli 1mg
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE, Source: E. coli 500ug
C101 Recombinant Human Apurinic-Apyrimidinic Endonuclease 1_APE, Source: E. coli 50μg
AE56100RA Rat DNA- (apurinic or apyrimidinic site) lyase (APEX1) ELISA Kit 48T
CSB-EL001900RA Rat DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase 500ug


 

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