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

Liver carboxylesterase 1 (Acyl-coenzyme A:cholesterol acyltransferase) (ACAT) (Brain carboxylesterase hBr1) (Carboxylesterase 1) (CE-1) (hCE-1) (EC 3.1.1.1) (Cocaine carboxylesterase) (Egasyn) (HMSE) (Methylumbelliferyl-acetate deacetylase 1) (EC 3.1.1.56) (Monocyte/macrophage serine esterase) (Retinyl ester hydrolase) (REH) (Serine esterase 1) (Triacylglycerol hydrolase) (TGH)

 EST1_HUMAN              Reviewed;         567 AA.
P23141; A6NIM1; A8K3K8; A8K844; E9PAU8; P82127; Q00015; Q13657;
Q14062; Q16737; Q16788; Q549X7; Q549X8; Q86UK2; Q96EE8; Q9UC52;
Q9UDG8; Q9UK77; Q9ULY2;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 2.
27-SEP-2017, entry version 184.
RecName: Full=Liver carboxylesterase 1;
AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase;
Short=ACAT;
AltName: Full=Brain carboxylesterase hBr1;
AltName: Full=Carboxylesterase 1;
Short=CE-1;
Short=hCE-1;
EC=3.1.1.1 {ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443, ECO:0000269|PubMed:9490062};
AltName: Full=Cocaine carboxylesterase;
AltName: Full=Egasyn;
AltName: Full=HMSE;
AltName: Full=Methylumbelliferyl-acetate deacetylase 1;
EC=3.1.1.56 {ECO:0000269|PubMed:9169443};
AltName: Full=Monocyte/macrophage serine esterase;
AltName: Full=Retinyl ester hydrolase;
Short=REH;
AltName: Full=Serine esterase 1;
AltName: Full=Triacylglycerol hydrolase;
Short=TGH;
Flags: Precursor;
Name=CES1; Synonyms=CES2, SES1;
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).
PubMed=1918003;
Munger J.S., Shi G.P., Mark E.A., Chin D.T., Gerard C., Chapman H.A.;
"A serine esterase released by human alveolar macrophages is closely
related to liver microsomal carboxylesterases.";
J. Biol. Chem. 266:18832-18838(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=8218228; DOI=10.1021/bi00094a018;
Kroetz D.L., McBride O.W., Gonzalez F.J.;
"Glycosylation-dependent activity of baculovirus-expressed human liver
carboxylesterases: cDNA cloning and characterization of two highly
similar enzyme forms.";
Biochemistry 32:11606-11617(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Peripheral blood, and Placenta;
PubMed=8406473; DOI=10.1006/geno.1993.1285;
Shibata F., Takagi Y., Kitajima M., Kuroda T., Omura T.;
"Molecular cloning and characterization of a human carboxylesterase
gene.";
Genomics 17:76-82(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8049197;
Becker A., Bottcher A., Lackner K.J., Fehringer P., Notka F.,
Aslanidis C., Schmitz G.;
"Purification, cloning, and expression of a human enzyme with acyl
coenzyme A: cholesterol acyltransferase activity, which is identical
to liver carboxylesterase.";
Arterioscler. Thromb. 14:1346-1355(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH BETA-GLUCURONIDASE.
TISSUE=Liver;
PubMed=10562416; DOI=10.1006/abbi.1999.1449;
Islam M.R., Waheed A., Shah G.N., Tomatsu S., Sly W.S.;
"Human egasyn binds beta-glucuronidase but neither the esterase active
site of egasyn nor the C-terminus of beta-glucuronidase is involved in
their interaction.";
Arch. Biochem. Biophys. 372:53-61(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Macrophage;
PubMed=11015575;
Ghosh S.;
"Cholesteryl ester hydrolase in human monocyte/macrophage: cloning,
sequencing, and expression of full-length cDNA.";
Physiol. Genomics 2:1-8(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 19-28.
TISSUE=Liver;
PubMed=11812220; DOI=10.1006/prep.2001.1553;
Alam M., Ho S., Vance D.E., Lehner R.;
"Heterologous expression, purification, and characterization of human
triacylglycerol hydrolase.";
Protein Expr. Purif. 24:33-42(2002).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Liver;
Hosokawa M., Yaginuma Y., Watanabe N., Yamamoto N., Tsukada E.,
Ohhata Y., Satoh T., Chiba K.;
"Inverted duplication of human carboxylesterase 1(CES1) genes, which
are difference in regulation at the transcriptional level.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Esophagus, and Heart;
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).
[10]
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Blood, and Lung;
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-429 (ISOFORM 1).
TISSUE=Brain;
PubMed=10518925; DOI=10.1016/S0014-5793(99)01111-4;
Mori M., Hosokawa M., Ogasawara Y., Tsukada E., Chiba K.;
"cDNA cloning, characterization and stable expression of novel human
brain carboxylesterase.";
FEBS Lett. 458:17-22(1999).
[13]
PROTEIN SEQUENCE OF 18-27; 37-52; 65-75; 187-198; 258-273; 288-298;
314-319; 340-352; 377-382; 439-461; 463-473; 499-504; 506-514 AND
539-557, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
AND SUBUNIT.
TISSUE=Liver;
PubMed=7980644; DOI=10.1016/0006-2952(94)90461-8;
Brzezinski M.R., Abraham T.L., Stone C.L., Dean R.A., Bosron W.F.;
"Purification and characterization of a human liver cocaine
carboxylesterase that catalyzes the production of benzoylecgonine and
the formation of cocaethylene from alcohol and cocaine.";
Biochem. Pharmacol. 48:1747-1755(1994).
[14]
PROTEIN SEQUENCE OF 18-28; 65-78; 93-107; 243-255; 258-266; 297-313
AND 341-346, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
PubMed=9490062; DOI=10.1046/j.1432-1327.1998.2510863.x;
Schindler R., Mentlein R., Feldheim W.;
"Purification and characterization of retinyl ester hydrolase as a
member of the non-specific carboxylesterase supergene family.";
Eur. J. Biochem. 251:863-873(1998).
[15]
PROTEIN SEQUENCE OF 19-34, NUCLEOTIDE SEQUENCE [MRNA] OF 113-121;
138-149; 216-224; 351-357 AND 466-471, AND SUBUNIT.
TISSUE=Liver;
PubMed=8597091; DOI=10.1016/0378-4274(95)03493-5;
Satoh T., Hosokawa M.;
"Molecular aspects of carboxylesterase isoforms in comparison with
other esterases.";
Toxicol. Lett. 82:439-445(1995).
[16]
PROTEIN SEQUENCE OF 19-28, ACTIVE SITES, GLYCOSYLATION AT ASN-79, AND
MUTAGENESIS OF ASN-79; SER-221; GLU-354; HIS-468 AND 564-HIS--LEU-567.
PubMed=12022871; DOI=10.1021/bi0255625;
Alam M., Vance D.E., Lehner R.;
"Structure-function analysis of human triacylglycerol hydrolase by
site-directed mutagenesis: identification of the catalytic triad and a
glycosylation site.";
Biochemistry 41:6679-6687(2002).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 61-567.
TISSUE=Liver;
PubMed=1997784; DOI=10.1016/0024-3205(91)90515-D;
Long R.M., Calabrese M.R., Martin B.M., Pohl L.R.;
"Cloning and sequencing of a human liver carboxylesterase isoenzyme.";
Life Sci. 48:PL43-PL49(1991).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 64-567, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2070086;
Zschunke F., Salmassi A., Kreipe H., Buck F., Parwaresch M.R.,
Radzun H.J.;
"cDNA cloning and characterization of human monocyte/macrophage serine
esterase-1.";
Blood 78:506-512(1991).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 114-567.
TISSUE=Liver;
PubMed=1748313; DOI=10.1016/0378-1119(91)90448-K;
Riddles P.W., Richards L.J., Bowles M.R., Pond S.M.;
"Cloning and analysis of a cDNA encoding a human liver
carboxylesterase.";
Gene 108:289-292(1991).
[20]
FUNCTION AS METHYLUMBELLIFERYL-ACETATE DEACETYLASE, CATALYTIC
ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9169443; DOI=10.1074/jbc.272.23.14769;
Pindel E.V., Kedishvili N.Y., Abraham T.L., Brzezinski M.R., Zhang J.,
Dean R.A., Bosron W.F.;
"Purification and cloning of a broad substrate specificity human liver
carboxylesterase that catalyzes the hydrolysis of cocaine and
heroin.";
J. Biol. Chem. 272:14769-14775(1997).
[21]
BIOPHYSICOCHEMICAL PROPERTIES, VARIANT GLU-143, AND CHARACTERIZATION
OF VARIANT GLU-143.
PubMed=18485328; DOI=10.1016/j.ajhg.2008.04.015;
Zhu H.-J., Patrick K.S., Yuan H.-J., Wang J.-S., Donovan J.L.,
DeVane C.L., Malcolm R., Johnson J.A., Youngblood G.L., Sweet D.H.,
Langaee T.Y., Markowitz J.S.;
"Two CES1 gene mutations lead to dysfunctional carboxylesterase 1
activity in man: clinical significance and molecular basis.";
Am. J. Hum. Genet. 82:1241-1248(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
PubMed=12725862; DOI=10.1016/S1074-5521(03)00071-1;
Bencharit S., Morton C.L., Hyatt J.L., Kuhn P., Danks M.K.,
Potter P.M., Redinbo M.R.;
"Crystal structure of human carboxylesterase 1 complexed with the
Alzheimer's drug tacrine. From binding promiscuity to selective
inhibition.";
Chem. Biol. 10:341-349(2003).
[25]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.
PubMed=12679808; DOI=10.1038/nsb919;
Bencharit S., Morton C.L., Xue Y., Potter P.M., Redinbo M.R.;
"Structural basis of heroin and cocaine metabolism by a promiscuous
human drug-processing enzyme.";
Nat. Struct. Biol. 10:349-356(2003).
-!- FUNCTION: Involved in the detoxification of xenobiotics and in the
activation of ester and amide prodrugs. Hydrolyzes aromatic and
aliphatic esters, but has no catalytic activity toward amides or a
fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine
to form benzoylecgonine. Catalyzes the transesterification of
cocaine to form cocaethylene. Displays fatty acid ethyl ester
synthase activity, catalyzing the ethyl esterification of oleic
acid to ethyloleate. {ECO:0000269|PubMed:7980644,
ECO:0000269|PubMed:9169443}.
-!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a
carboxylate. {ECO:0000255|PROSITE-ProRule:PRU10039,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062}.
-!- CATALYTIC ACTIVITY: 4-methylumbelliferyl acetate + H(2)O = 4-
methylumbelliferone + acetate. {ECO:0000269|PubMed:9169443}.
-!- ENZYME REGULATION: Activated by CHAPS.
{ECO:0000269|PubMed:9490062}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=106.6 uM for p-nitrophenyl acetate
{ECO:0000269|PubMed:18485328, ECO:0000269|PubMed:7980644,
ECO:0000269|PubMed:9169443, ECO:0000269|PubMed:9490062};
KM=775.7 uM for L-methylphenidate {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
KM=663.5 uM for D-methylphenidate {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
KM=116 uM for cocaine {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
KM=43 mM for ethanol {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
KM=0.8 mM for 4-methylumbelliferyl acetate
{ECO:0000269|PubMed:18485328, ECO:0000269|PubMed:7980644,
ECO:0000269|PubMed:9169443, ECO:0000269|PubMed:9490062};
KM=6.3 mM for heroin {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
KM=8.3 mM for 6-monoacetylmorphine {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
Vmax=493.9 nmol/min/mg enzyme with p-nitrophenyl acetate as
substrate {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
Vmax=1701.1 pmol/min/mg enzyme with L-methylphenidate as
substrate {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
Vmax=177.2 pmol/min/mg enzyme with D-methylphenidate as
substrate {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:18485328,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:9169443,
ECO:0000269|PubMed:9490062};
-!- SUBUNIT: Homotrimer and homohexamer. Binds to beta-glucuronidase.
{ECO:0000269|PubMed:12679808, ECO:0000269|PubMed:12725862,
ECO:0000269|PubMed:7980644, ECO:0000269|PubMed:8597091}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:10562416}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P23141-1; Sequence=Displayed;
Name=2;
IsoId=P23141-2; Sequence=VSP_021026;
Name=3;
IsoId=P23141-3; Sequence=VSP_047158;
-!- TISSUE SPECIFICITY: Expressed predominantly in liver with lower
levels in heart and lung. {ECO:0000269|PubMed:10562416}.
-!- PTM: Contains sialic acid.
-!- PTM: Cleavage of the signal sequence can occur at 2 positions,
either between Trp-17 and Gly-18 or between Gly-18 and His-19.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA83932.1; Type=Frameshift; Positions=301, 312, 318, 383, 391; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M73499; AAA35649.1; -; mRNA.
EMBL; L07764; AAA16036.1; -; mRNA.
EMBL; L07765; AAA35711.1; -; mRNA.
EMBL; D21088; BAA04650.1; -; Genomic_DNA.
EMBL; S73751; AAC60631.2; -; mRNA.
EMBL; AF177775; AAD53175.1; -; mRNA.
EMBL; AY268104; AAP20868.1; -; mRNA.
EMBL; AB119995; BAC87748.1; -; mRNA.
EMBL; AB119996; BAC87749.1; -; mRNA.
EMBL; AB119997; BAC87750.1; -; Genomic_DNA.
EMBL; AB119998; BAC87751.1; -; Genomic_DNA.
EMBL; AK290623; BAF83312.1; -; mRNA.
EMBL; AK292209; BAF84898.1; -; mRNA.
EMBL; AC147362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012418; AAH12418.1; -; mRNA.
EMBL; BC110338; AAI10339.1; -; mRNA.
EMBL; AB025026; BAA84995.1; -; mRNA.
EMBL; M55509; AAA35650.1; -; mRNA.
EMBL; X52973; CAA37147.1; -; mRNA.
EMBL; M65261; AAA83932.1; ALT_FRAME; mRNA.
CCDS; CCDS32450.1; -. [P23141-2]
CCDS; CCDS45488.1; -. [P23141-1]
CCDS; CCDS45489.1; -. [P23141-3]
PIR; A41010; A41010.
RefSeq; NP_001020365.1; NM_001025194.1. [P23141-1]
RefSeq; NP_001020366.1; NM_001025195.1. [P23141-2]
RefSeq; NP_001257.4; NM_001266.4. [P23141-3]
UniGene; Hs.558865; -.
PDB; 1MX1; X-ray; 2.40 A; A/B/C/D/E/F=19-567.
PDB; 1MX5; X-ray; 2.80 A; A/B/C/D/E/F=19-567.
PDB; 1MX9; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=19-567.
PDB; 1YA4; X-ray; 3.20 A; A/B/C=21-552.
PDB; 1YA8; X-ray; 3.00 A; A/B/C=21-552.
PDB; 1YAH; X-ray; 3.00 A; A/B/C=21-552.
PDB; 1YAJ; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=21-552.
PDB; 2DQY; X-ray; 3.00 A; A/B/C=19-561.
PDB; 2DQZ; X-ray; 2.80 A; A/B/C=19-561.
PDB; 2DR0; X-ray; 3.20 A; A/B/C=19-561.
PDB; 2H7C; X-ray; 2.00 A; A/B/C/D/E/F=19-561.
PDB; 2HRQ; X-ray; 2.70 A; A/B/C/D/E/F=21-553.
PDB; 2HRR; X-ray; 2.70 A; A/B/C=21-553.
PDB; 3K9B; X-ray; 3.10 A; A/B/C=24-553.
PDB; 4AB1; X-ray; 2.20 A; A=21-553.
PDB; 5A7F; X-ray; 1.86 A; A=21-553.
PDB; 5A7G; X-ray; 1.48 A; A=21-553.
PDB; 5A7H; X-ray; 2.01 A; A=22-553.
PDBsum; 1MX1; -.
PDBsum; 1MX5; -.
PDBsum; 1MX9; -.
PDBsum; 1YA4; -.
PDBsum; 1YA8; -.
PDBsum; 1YAH; -.
PDBsum; 1YAJ; -.
PDBsum; 2DQY; -.
PDBsum; 2DQZ; -.
PDBsum; 2DR0; -.
PDBsum; 2H7C; -.
PDBsum; 2HRQ; -.
PDBsum; 2HRR; -.
PDBsum; 3K9B; -.
PDBsum; 4AB1; -.
PDBsum; 5A7F; -.
PDBsum; 5A7G; -.
PDBsum; 5A7H; -.
ProteinModelPortal; P23141; -.
SMR; P23141; -.
BioGrid; 107494; 11.
IntAct; P23141; 8.
MINT; MINT-5004142; -.
STRING; 9606.ENSP00000353720; -.
BindingDB; P23141; -.
ChEMBL; CHEMBL2265; -.
DrugBank; DB03056; 4-Piperidino-Piperidine.
DrugBank; DB01086; Benzocaine.
DrugBank; DB01101; Capecitabine.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB01410; Ciclesonide.
DrugBank; DB00758; Clopidogrel.
DrugBank; DB04838; Cyclandelate.
DrugBank; DB06695; Dabigatran etexilate.
DrugBank; DB02161; Hydroxy-Phenyl-Acetic Acid 8-Methyl-8-Aza-Bicyclo[3.2.1]Oct-3-Yl Ester.
DrugBank; DB00328; Indomethacin.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00583; L-Carnitine.
DrugBank; DB06693; Mevastatin.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DrugBank; DB04509; N-Methylnaloxonium.
DrugBank; DB00198; Oseltamivir.
DrugBank; DB09269; Phenylacetic acid.
DrugBank; DB01599; Probucol.
DrugBank; DB06201; Rufinamide.
DrugBank; DB11362; Selexipag.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB04795; Thenoyltrifluoroacetone.
DrugBank; DB00519; Trandolapril.
GuidetoPHARMACOLOGY; 2592; -.
SwissLipids; SLP:000001265; -.
ESTHER; human-CES1; Carb_B_Chordata.
MEROPS; S09.982; -.
iPTMnet; P23141; -.
PhosphoSitePlus; P23141; -.
BioMuta; CES1; -.
DMDM; 119576; -.
MaxQB; P23141; -.
PaxDb; P23141; -.
PeptideAtlas; P23141; -.
PRIDE; P23141; -.
DNASU; 1066; -.
Ensembl; ENST00000360526; ENSP00000353720; ENSG00000198848. [P23141-2]
Ensembl; ENST00000361503; ENSP00000355193; ENSG00000198848. [P23141-1]
Ensembl; ENST00000422046; ENSP00000390492; ENSG00000198848. [P23141-3]
Ensembl; ENST00000571922; ENSP00000460045; ENSG00000262243.
Ensembl; ENST00000574513; ENSP00000461208; ENSG00000262243.
Ensembl; ENST00000576783; ENSP00000458586; ENSG00000262243.
GeneID; 1066; -.
KEGG; hsa:1066; -.
UCSC; uc002eil.4; human. [P23141-1]
CTD; 1066; -.
DisGeNET; 1066; -.
EuPathDB; HostDB:ENSG00000198848.12; -.
GeneCards; CES1; -.
HGNC; HGNC:1863; CES1.
HPA; HPA012023; -.
HPA; HPA046717; -.
MIM; 114835; gene+phenotype.
neXtProt; NX_P23141; -.
OpenTargets; ENSG00000198848; -.
PharmGKB; PA107; -.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
GeneTree; ENSGT00760000118946; -.
HOVERGEN; HBG008839; -.
InParanoid; P23141; -.
KO; K01044; -.
OMA; SEPRYDG; -.
OrthoDB; EOG091G03ZC; -.
PhylomeDB; P23141; -.
TreeFam; TF315470; -.
BioCyc; MetaCyc:HS11616-MONOMER; -.
BRENDA; 3.1.1.1; 2681.
Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
SABIO-RK; P23141; -.
ChiTaRS; CES1; human.
EvolutionaryTrace; P23141; -.
GeneWiki; Carboxylesterase_1; -.
GenomeRNAi; 1066; -.
PRO; PR:P23141; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000198848; -.
CleanEx; HS_CES1; -.
CleanEx; HS_CES2; -.
ExpressionAtlas; P23141; baseline and differential.
Genevisible; P23141; HS.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0052689; F:carboxylic ester hydrolase activity; TAS:Reactome.
GO; GO:0047374; F:methylumbelliferyl-acetate deacetylase activity; IEA:UniProtKB-EC.
GO; GO:0004771; F:sterol esterase activity; IDA:BHF-UCL.
GO; GO:0006695; P:cholesterol biosynthetic process; IDA:BHF-UCL.
GO; GO:0090122; P:cholesterol ester hydrolysis involved in cholesterol transport; TAS:BHF-UCL.
GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
GO; GO:0051791; P:medium-chain fatty acid metabolic process; IDA:BHF-UCL.
GO; GO:0008152; P:metabolic process; TAS:ProtInc.
GO; GO:0009636; P:response to toxic substance; TAS:ProtInc.
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.
InterPro; IPR019819; Carboxylesterase_B_CS.
Pfam; PF00135; COesterase; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Hydrolase; Phosphoprotein; Polymorphism;
Reference proteome; Serine esterase; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:7980644,
ECO:0000269|PubMed:9490062}.
CHAIN 18 567 Liver carboxylesterase 1.
/FTId=PRO_0000391359.
ACT_SITE 221 221 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039,
ECO:0000269|PubMed:12022871}.
ACT_SITE 354 354 Charge relay system.
{ECO:0000269|PubMed:12022871}.
ACT_SITE 468 468 Charge relay system.
{ECO:0000269|PubMed:12022871}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12022871}.
DISULFID 87 116
DISULFID 274 285
VAR_SEQ 17 17 W -> WA (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8218228}.
/FTId=VSP_021026.
VAR_SEQ 362 362 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_047158.
VARIANT 18 18 G -> GA.
/FTId=VAR_002357.
VARIANT 75 75 S -> N (in dbSNP:rs2307240).
/FTId=VAR_014314.
VARIANT 143 143 G -> E (5.4-fold decrease in activity
with p-nitrophenyl acetate as substrate;
no change in affinity for p-nitrophenyl
acetate; loss of activity with L- or D-
methylphenidate as substrate;
dbSNP:rs71647871).
{ECO:0000269|PubMed:18485328}.
/FTId=VAR_046954.
VARIANT 199 199 R -> H (in dbSNP:rs2307243).
/FTId=VAR_014594.
VARIANT 203 203 D -> E (in dbSNP:rs2307227).
/FTId=VAR_014595.
MUTAGEN 79 79 N->A: Abolishes glycosylation.
{ECO:0000269|PubMed:12022871}.
MUTAGEN 221 221 S->A: Loss of activity.
{ECO:0000269|PubMed:12022871}.
MUTAGEN 354 354 E->A: Loss of activity.
{ECO:0000269|PubMed:12022871}.
MUTAGEN 468 468 H->A: Loss of activity.
{ECO:0000269|PubMed:12022871}.
MUTAGEN 564 567 Missing: Does not result in secretion.
{ECO:0000269|PubMed:12022871}.
CONFLICT 2 2 W -> L (in Ref. 5; AAD53175).
{ECO:0000305}.
CONFLICT 4 7 RAFI -> PALV (in Ref. 3; BAA04650, 8;
BAC87749/BAC87751, 9; BAF83312/BAF84898
and 11; AAH12418). {ECO:0000305}.
CONFLICT 12 12 S -> A (in Ref. 3; BAA04650, 8; BAC87749/
BAC87751, 9; BAF83312/BAF84898 and 11;
AAH12418). {ECO:0000305}.
CONFLICT 19 21 HPS -> GPP (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 19 19 H -> N (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 21 24 SSPP -> EAVV (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 27 28 DT -> AK (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 28 29 TV -> DT (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 56 56 A -> G (in Ref. 2; AAA16036/AAA35711).
{ECO:0000305}.
CONFLICT 64 64 R -> G (in Ref. 18; CAA37147).
{ECO:0000305}.
CONFLICT 65 65 F -> S (in Ref. 6; AAP20868).
{ECO:0000305}.
CONFLICT 75 75 S -> A (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 78 78 K -> I (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 Q -> R (in Ref. 6; AAP20868).
{ECO:0000305}.
CONFLICT 98 98 S -> F (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 105 107 KEN -> PAD (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 115 115 D -> H (in Ref. 19; AAA83932).
{ECO:0000305}.
CONFLICT 186 186 R -> G (in Ref. 18; CAA37147).
{ECO:0000305}.
CONFLICT 247 247 S -> I (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 251 251 L -> K (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 253 253 S -> G (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 255 255 L -> P (in Ref. 9; BAF83312).
{ECO:0000305}.
CONFLICT 258 258 K -> Q (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 281 281 V -> A (in Ref. 19; AAA83932).
{ECO:0000305}.
CONFLICT 298 298 T -> I (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 302 302 K -> A (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 305 305 S -> M (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 337 337 A -> R (in Ref. 19; AAA83932).
{ECO:0000305}.
CONFLICT 417 417 F -> I (in Ref. 19; AAA83932).
{ECO:0000305}.
CONFLICT 512 512 E -> K (in Ref. 19; AAA83932).
{ECO:0000305}.
CONFLICT 536 536 A -> G (in Ref. 2; AAA16036/AAA35711).
{ECO:0000305}.
CONFLICT 563 563 E -> D (in Ref. 19; AAA83932).
{ECO:0000305}.
STRAND 25 28 {ECO:0000244|PDB:5A7G}.
STRAND 31 34 {ECO:0000244|PDB:5A7G}.
STRAND 36 38 {ECO:0000244|PDB:5A7G}.
STRAND 47 54 {ECO:0000244|PDB:5A7G}.
HELIX 61 63 {ECO:0000244|PDB:5A7G}.
STRAND 75 79 {ECO:0000244|PDB:5A7G}.
STRAND 86 88 {ECO:0000244|PDB:5A7G}.
HELIX 91 101 {ECO:0000244|PDB:5A7G}.
STRAND 104 106 {ECO:0000244|PDB:5A7G}.
STRAND 112 114 {ECO:0000244|PDB:5A7G}.
STRAND 118 123 {ECO:0000244|PDB:5A7G}.
TURN 127 130 {ECO:0000244|PDB:4AB1}.
STRAND 133 139 {ECO:0000244|PDB:5A7G}.
TURN 143 145 {ECO:0000244|PDB:5A7G}.
HELIX 149 151 {ECO:0000244|PDB:5A7G}.
HELIX 155 161 {ECO:0000244|PDB:5A7G}.
STRAND 164 168 {ECO:0000244|PDB:5A7G}.
HELIX 173 177 {ECO:0000244|PDB:5A7G}.
HELIX 183 185 {ECO:0000244|PDB:2HRQ}.
HELIX 189 204 {ECO:0000244|PDB:5A7G}.
HELIX 205 208 {ECO:0000244|PDB:5A7G}.
STRAND 210 220 {ECO:0000244|PDB:5A7G}.
HELIX 222 231 {ECO:0000244|PDB:5A7G}.
HELIX 234 236 {ECO:0000244|PDB:5A7G}.
TURN 237 239 {ECO:0000244|PDB:1MX9}.
STRAND 241 247 {ECO:0000244|PDB:5A7G}.
HELIX 253 255 {ECO:0000244|PDB:5A7G}.
HELIX 262 272 {ECO:0000244|PDB:5A7G}.
HELIX 279 288 {ECO:0000244|PDB:5A7G}.
HELIX 291 301 {ECO:0000244|PDB:5A7G}.
TURN 302 304 {ECO:0000244|PDB:5A7G}.
STRAND 308 310 {ECO:0000244|PDB:5A7G}.
HELIX 312 314 {ECO:0000244|PDB:5A7F}.
STRAND 325 327 {ECO:0000244|PDB:5A7G}.
HELIX 332 338 {ECO:0000244|PDB:5A7G}.
STRAND 339 341 {ECO:0000244|PDB:2H7C}.
STRAND 346 351 {ECO:0000244|PDB:5A7G}.
TURN 352 355 {ECO:0000244|PDB:2HRQ}.
HELIX 358 361 {ECO:0000244|PDB:5A7G}.
TURN 363 365 {ECO:0000244|PDB:1MX9}.
STRAND 369 371 {ECO:0000244|PDB:1MX5}.
HELIX 375 384 {ECO:0000244|PDB:5A7G}.
HELIX 386 389 {ECO:0000244|PDB:5A7G}.
HELIX 393 395 {ECO:0000244|PDB:5A7G}.
HELIX 396 404 {ECO:0000244|PDB:5A7G}.
HELIX 410 425 {ECO:0000244|PDB:5A7G}.
HELIX 427 439 {ECO:0000244|PDB:5A7G}.
STRAND 444 450 {ECO:0000244|PDB:5A7G}.
STRAND 458 460 {ECO:0000244|PDB:1MX5}.
TURN 468 471 {ECO:0000244|PDB:5A7G}.
HELIX 472 475 {ECO:0000244|PDB:5A7G}.
HELIX 478 480 {ECO:0000244|PDB:5A7G}.
HELIX 487 506 {ECO:0000244|PDB:5A7G}.
STRAND 521 523 {ECO:0000244|PDB:2DQZ}.
STRAND 525 532 {ECO:0000244|PDB:5A7G}.
STRAND 534 537 {ECO:0000244|PDB:5A7G}.
HELIX 541 551 {ECO:0000244|PDB:5A7G}.
SEQUENCE 567 AA; 62521 MW; D3A00BDCDC7E5DFF CRC64;
MWLRAFILAT LSASAAWGHP SSPPVVDTVH GKVLGKFVSL EGFAQPVAIF LGIPFAKPPL
GPLRFTPPQP AEPWSFVKNA TSYPPMCTQD PKAGQLLSEL FTNRKENIPL KLSEDCLYLN
IYTPADLTKK NRLPVMVWIH GGGLMVGAAS TYDGLALAAH ENVVVVTIQY RLGIWGFFST
GDEHSRGNWG HLDQVAALRW VQDNIASFGG NPGSVTIFGE SAGGESVSVL VLSPLAKNLF
HRAISESGVA LTSVLVKKGD VKPLAEQIAI TAGCKTTTSA VMVHCLRQKT EEELLETTLK
MKFLSLDLQG DPRESQPLLG TVIDGMLLLK TPEELQAERN FHTVPYMVGI NKQEFGWLIP
MQLMSYPLSE GQLDQKTAMS LLWKSYPLVC IAKELIPEAT EKYLGGTDDT VKKKDLFLDL
IADVMFGVPS VIVARNHRDA GAPTYMYEFQ YRPSFSSDMK PKTVIGDHGD ELFSVFGAPF
LKEGASEEEI RLSKMVMKFW ANFARNGNPN GEGLPHWPEY NQKEGYLQIG ANTQAAQKLK
DKEVAFWTNL FAKKAVEKPP QTEHIEL


Related products :

Catalog number Product name Quantity
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
EIAAB13343 Carboxyesterase ES-1,E1,Es2,Esterase-2,ES-THET,Liver carboxylesterase 1,Neutral retinyl ester hydrolase,NREH,Rat,Rattus norvegicus,REH,Retinyl ester hydrolase
GWB-9FBB60 Anti- CES1 (carboxylesterase 1 (monocyte macrophage serine esterase 1)) Antibody
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
GWB-6A4D8C Carboxylesterase 1 (monocyte macrophage Serine Esterase 1) (CES1) Goat anti-Human Polyclonal (Internal) Antibody
EIAAB13344 Egasyn,Es22,Es-22,Esterase-22,Liver carboxylesterase 22,Mouse,Mus musculus
EIAAB13338 Acyl-coenzyme A cholesterol acyltransferase,Ces1,ES-x,Liver carboxylesterase 1,Mouse,Mus musculus
CES3 CES1 Gene carboxylesterase 1 (monocyte_macrophage serine esterase 1)
201-20-1029 CES1{carboxylesterase 1 (monocyte_macrophage serine esterase 1)}rabbit.pAb 0.1ml
GWB-9FBB60 Anti- CES1 (carboxylesterase 1 (monocyte_macrophage serine esterase 1)) Antibody
EIAAB06893 CES1P1,CES4,Homo sapiens,Human,Inactive carboxylesterase 1 pseudogene 1,PCE-3,Placental carboxylesterase 3,Putative inactive carboxylesterase 4
EIAAB13346 Carboxylesterase 3,CES3,Homo sapiens,Human,Liver carboxylesterase 31 homolog,UNQ869_PRO1887
GWB-6A4D8C Carboxylesterase 1 (monocyte_macrophage Serine Esterase 1) (CES1) Goat anti-Human Polyclonal (Internal) Antibody
CSB-EL005258RA Rat carboxylesterase 1 (monocyte_macrophage serine esterase 1) (CES1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB13342 Carboxylesterase 2,CE-2,CES2,Cocaine esterase,hCE-2,Homo sapiens,Human,ICE
EIAAB06894 Carboxylesterase 3,Ces1,Ces3,FAEE synthase,Fatty acid ethyl ester synthase,Mouse,Mus musculus,TGH,Triacylglycerol hydrolase
EIAAB13347 Es31,ES-male,Esterase-31,Liver carboxylesterase 31,Mouse,Mus musculus
CSB-EL005258MO Mouse carboxylesterase 1 (monocyte_macrophage serine esterase 1) (CES1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL005258HU Human carboxylesterase 1 (monocyte_macrophage serine esterase 1) (CES1) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB13345 Carboxyesterase ES-3,Ces1,ES-HTEL,Liver carboxylesterase 3,pI 5.5 esterase,Rat,Rattus norvegicus
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
CSB-PA005258GA01HU Rabbit anti-human carboxylesterase 1 (monocyte_macrophage serine esterase 1) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA005258GA01HU Rabbit anti-human carboxylesterase 1 (monocyte_macrophage serine esterase 1) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
EIAAB13351 Carboxylesterase 5A,Carboxylesterase-like urinary excreted protein homolog,Cauxin,Ces5a,Ces7,Epididymis-specific gene 615 protein,Rat,Rattus norvegicus


 

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