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

Carboxylesterase 3 (EC 3.1.1.1) (Liver carboxylesterase 31 homolog)

 EST3_HUMAN              Reviewed;         571 AA.
Q6UWW8; B2Z3W9; F5H242; Q7Z6J1; Q9H6X7;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 121.
RecName: Full=Carboxylesterase 3;
EC=3.1.1.1;
AltName: Full=Liver carboxylesterase 31 homolog;
Flags: Precursor;
Name=CES3; ORFNames=UNQ869/PRO1887;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, TISSUE
SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
PubMed=15100172; DOI=10.1124/dmd.32.5.505;
Sanghani S.P., Quinney S.K., Fredenburg T.B., Davis W.I., Murry D.J.,
Bosron W.F.;
"Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-
[4-N-(5-aminopentanoic acid)-1-piperidino] carbonyloxycamptothecin and
7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin, by
human carboxylesterases CES1A1, CES2, and a newly expressed
carboxylesterase isoenzyme, CES3.";
Drug Metab. Dispos. 32:505-511(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon mucosa;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-129; THR-151;
HIS-160; LYS-191; ASN-213; TRP-367; VAL-523 AND VAL-555.
NIEHS SNPs program;
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
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).
[8]
TISSUE SPECIFICITY.
PubMed=14581373;
Sanghani S.P., Quinney S.K., Fredenburg T.B., Sun Z., Davis W.I.,
Murry D.J., Cummings O.W., Seitz D.E., Bosron W.F.;
"Carboxylesterases expressed in human colon tumor tissue and their
role in CPT-11 hydrolysis.";
Clin. Cancer Res. 9:4983-4991(2003).
[9]
TISSUE SPECIFICITY.
PubMed=15687373; DOI=10.1124/jpet.104.081265;
Quinney S.K., Sanghani S.P., Davis W.I., Hurley T.D., Sun Z.,
Murry D.J., Bosron W.F.;
"Hydrolysis of capecitabine to 5'-deoxy-5-fluorocytidine by human
carboxylesterases and inhibition by loperamide.";
J. Pharmacol. Exp. Ther. 313:1011-1016(2005).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
-!- FUNCTION: Involved in the detoxification of xenobiotics and in the
activation of ester and amide prodrugs. Shows low catalytic
efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)-
1-piperidino]-carbonyloxycamptothecin), a prodrug for camptothecin
used in cancer therapeutics.
-!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a
carboxylate. {ECO:0000255|PROSITE-ProRule:PRU10039}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=137 uM for 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-
carbonyloxycamptothecin {ECO:0000269|PubMed:15100172};
KM=460 uM for 7-ethyl-10-[4-(1-piperidino)-1-amino]-
carbonyloxycamptothecin {ECO:0000269|PubMed:15100172};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6UWW8-1; Sequence=Displayed;
Name=2;
IsoId=Q6UWW8-2; Sequence=VSP_044994;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in liver, colon and small intestine.
{ECO:0000269|PubMed:14581373, ECO:0000269|PubMed:15100172,
ECO:0000269|PubMed:15687373}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15100172,
ECO:0000269|PubMed:19159218}.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ces3/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY358609; AAQ88972.1; -; mRNA.
EMBL; AK025389; BAB15123.1; -; mRNA.
EMBL; EU595874; ACD11491.1; -; Genomic_DNA.
EMBL; AC009084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83060.1; -; Genomic_DNA.
EMBL; BC053670; AAH53670.1; -; mRNA.
CCDS; CCDS10826.1; -. [Q6UWW8-1]
CCDS; CCDS54023.1; -. [Q6UWW8-2]
RefSeq; NP_001172105.1; NM_001185176.1. [Q6UWW8-2]
RefSeq; NP_001172106.1; NM_001185177.1.
RefSeq; NP_079198.2; NM_024922.5. [Q6UWW8-1]
UniGene; Hs.268700; -.
ProteinModelPortal; Q6UWW8; -.
SMR; Q6UWW8; -.
BioGrid; 117043; 10.
IntAct; Q6UWW8; 1.
STRING; 9606.ENSP00000304782; -.
ESTHER; human-CES3; Carb_B_Chordata.
MEROPS; S09.958; -.
iPTMnet; Q6UWW8; -.
PhosphoSitePlus; Q6UWW8; -.
BioMuta; CES3; -.
DMDM; 74758561; -.
EPD; Q6UWW8; -.
MaxQB; Q6UWW8; -.
PaxDb; Q6UWW8; -.
PeptideAtlas; Q6UWW8; -.
PRIDE; Q6UWW8; -.
Ensembl; ENST00000303334; ENSP00000304782; ENSG00000172828. [Q6UWW8-1]
Ensembl; ENST00000543856; ENSP00000445559; ENSG00000172828. [Q6UWW8-2]
GeneID; 23491; -.
KEGG; hsa:23491; -.
UCSC; uc002eqt.4; human. [Q6UWW8-1]
CTD; 23491; -.
DisGeNET; 23491; -.
EuPathDB; HostDB:ENSG00000172828.12; -.
GeneCards; CES3; -.
HGNC; HGNC:1865; CES3.
HPA; HPA041008; -.
HPA; HPA041307; -.
MIM; 605279; gene.
neXtProt; NX_Q6UWW8; -.
OpenTargets; ENSG00000172828; -.
PharmGKB; PA26418; -.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
GeneTree; ENSGT00760000118946; -.
HOGENOM; HOG000091866; -.
HOVERGEN; HBG008839; -.
InParanoid; Q6UWW8; -.
KO; K15743; -.
OMA; NWGFLDV; -.
OrthoDB; EOG091G03ZC; -.
PhylomeDB; Q6UWW8; -.
TreeFam; TF315470; -.
BioCyc; MetaCyc:HS10576-MONOMER; -.
Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
Reactome; R-HSA-8964038; LDL clearance.
SABIO-RK; Q6UWW8; -.
GeneWiki; Carboxylesterase_3; -.
GenomeRNAi; 23491; -.
PRO; PR:Q6UWW8; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000172828; -.
CleanEx; HS_CES3; -.
ExpressionAtlas; Q6UWW8; baseline and differential.
Genevisible; Q6UWW8; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
Pfam; PF00135; COesterase; 1.
SUPFAM; SSF53474; SSF53474; 2.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Hydrolase; Polymorphism;
Reference proteome; Serine esterase; Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 571 Carboxylesterase 3.
/FTId=PRO_0000305191.
MOTIF 568 571 Prevents secretion from ER.
{ECO:0000255}.
ACT_SITE 229 229 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039}.
ACT_SITE 347 347 Charge relay system. {ECO:0000250}.
ACT_SITE 460 460 Charge relay system. {ECO:0000250}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 97 124 {ECO:0000250}.
DISULFID 281 292 {ECO:0000250}.
VAR_SEQ 1 361 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044994.
VARIANT 129 129 V -> I (in dbSNP:rs61745806).
{ECO:0000269|Ref.4}.
/FTId=VAR_060699.
VARIANT 151 151 A -> T (in dbSNP:rs71647891).
{ECO:0000269|Ref.4}.
/FTId=VAR_060700.
VARIANT 160 160 Y -> H (in dbSNP:rs71647892).
{ECO:0000269|Ref.4}.
/FTId=VAR_060701.
VARIANT 191 191 E -> K (in dbSNP:rs61742964).
{ECO:0000269|Ref.4}.
/FTId=VAR_060702.
VARIANT 213 213 I -> N (in dbSNP:rs71647894).
{ECO:0000269|Ref.4}.
/FTId=VAR_060703.
VARIANT 367 367 R -> W (in dbSNP:rs61743167).
{ECO:0000269|Ref.4}.
/FTId=VAR_060704.
VARIANT 523 523 A -> V (in dbSNP:rs71649615).
{ECO:0000269|Ref.4}.
/FTId=VAR_060705.
VARIANT 555 555 I -> V (in dbSNP:rs8059252).
{ECO:0000269|Ref.4}.
/FTId=VAR_060706.
CONFLICT 372 372 A -> S (in Ref. 3; BAB15123).
{ECO:0000305}.
CONFLICT 481 483 Missing (in Ref. 7; AAH53670).
{ECO:0000305}.
SEQUENCE 571 AA; 62282 MW; F2200968FDE072D2 CRC64;
MERAVRVESG VLVGVVCLLL ACPATATGPE VAQPEVDTTL GRVRGRQVGV KGTDRLVNVF
LGIPFAQPPL GPDRFSAPHP AQPWEGVRDA STAPPMCLQD VESMNSSRFV LNGKQQIFSV
SEDCLVLNVY SPAEVPAGSG RPVMVWVHGG ALITGAATSY DGSALAAYGD VVVVTVQYRL
GVLGFFSTGD EHAPGNQGFL DVVAALRWVQ ENIAPFGGDL NCVTVFGGSA GGSIISGLVL
SPVAAGLFHR AITQSGVITT PGIIDSHPWP LAQKIANTLA CSSSSPAEMV QCLQQKEGEE
LVLSKKLKNT IYPLTVDGTV FPKSPKELLK EKPFHSVPFL MGVNNHEFSW LIPRGWGLLD
TMEQMSREDM LAISTPVLTS LDVPPEMMPT VIDEYLGSNS DAQAKCQAFQ EFMGDVFINV
PTVSFSRYLR DSGSPVFFYE FQHRPSSFAK IKPAWVKADH GAEGAFVFGG PFLMDESSRL
AFPEATEEEK QLSLTMMAQW THFARTGDPN SKALPPWPQF NQAEQYLEIN PVPRAGQKFR
EAWMQFWSET LPSKIQQWHQ KQKNRKAQED L


Related products :

Catalog number Product name Quantity
EIAAB13346 Carboxylesterase 3,CES3,Homo sapiens,Human,Liver carboxylesterase 31 homolog,UNQ869_PRO1887
EIAAB13337 ACAT,Acyl-coenzyme A cholesterol acyltransferase,Brain carboxylesterase hBr1,CES1,CES2,Cocaine carboxylesterase,Egasyn,HMSE,Homo sapiens,Human,Liver carboxylesterase 1,Monocyte_macrophage serine ester
EIAAB13353 Carboxylesterase 5A,Carboxylesterase-like urinary excreted protein homolog,Cauxin,Ces5a,Ces7,Mouse,Mus musculus
EIAAB13352 Carboxylesterase 5A,Carboxylesterase-like urinary excreted protein homolog,Cauxin,CES5A,CES7,Homo sapiens,Human
EIAAB06893 CES1P1,CES4,Homo sapiens,Human,Inactive carboxylesterase 1 pseudogene 1,PCE-3,Placental carboxylesterase 3,Putative inactive carboxylesterase 4
EIAAB06895 Carboxyesterase ES-10,Carboxylesterase 3,Ces3,ES-HVEL,FAEE synthase,Fatty acid ethyl ester synthase,Liver carboxylesterase 10,pI 6.1 esterase,Rat,Rattus norvegicus
EIAAB13351 Carboxylesterase 5A,Carboxylesterase-like urinary excreted protein homolog,Cauxin,Ces5a,Ces7,Epididymis-specific gene 615 protein,Rat,Rattus norvegicus
EIAAB13354 Canis familiaris,Canis lupus familiaris,Carboxylesterase 5A,Carboxylesterase-like urinary excreted protein homolog,Cauxin,CES5A,CES7,Dog
YF-PA10902 anti-Liver Carboxylesterase 1 50 ug
NBL1-09112 Liver Carboxylesterase 1 Lysate 0.1 mg
NBL1-09113 Liver Carboxylesterase 1 Lysate 0.1 mg
CSB-EL005258RA Rat Liver carboxylesterase 1(CES1) ELISA kit 96T
CSB-EL005258MO Mouse Liver carboxylesterase 1(CES1) ELISA kit 96T
CETN1 CES2 Gene carboxylesterase 2 (intestine, liver)
CSB-EL005258HU Human Liver carboxylesterase 1(CES1) ELISA kit 96T
201-20-1030 CES2{carboxylesterase 2 (intestine, liver)}rabbit.pAb 0.1ml
EIAAB13297 Gm4738,Liver carboxylesterase 31-like,Mouse,Mus musculus
CSB-EL005258RA Rat Liver carboxylesterase 1(CES1) ELISA kit SpeciesRat 96T
CSB-EL005258HU Human Liver carboxylesterase 1(CES1) ELISA kit SpeciesHuman 96T
GWB-92D165 Anti- CES2 (carboxylesterase 2 (intestine. liver)) Antibody
ESTN_MOUSE ELISA Kit FOR Liver carboxylesterase N; organism: Mouse; gene name: Es1 96T
abx111386 Polyclonal Rabbit Carboxylesterase 2 (Intestine, Liver) Antibody 50 μl
CSB-EL005258MO Mouse Liver carboxylesterase 1(CES1) ELISA kit SpeciesMouse 96T
EIAAB13341 CES2,ICE,Liver carboxylesterase 2,Oryctolagus cuniculus,Rabbit
EIAAB13360 Es1,Liver carboxylesterase N,Lung surfactant convertase,Mouse,Mus musculus,PES-N


 

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