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Angiotensin-converting enzyme 2 (EC 3.4.17.23) (ACE-related carboxypeptidase) (Angiotensin-converting enzyme homolog) (ACEH) (Metalloprotease MPROT15) [Cleaved into: Processed angiotensin-converting enzyme 2]

 ACE2_HUMAN              Reviewed;         805 AA.
Q9BYF1; C7ECU1; Q6UWP0; Q86WT0; Q9NRA7; Q9UFZ6;
02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
02-AUG-2005, sequence version 2.
25-OCT-2017, entry version 160.
RecName: Full=Angiotensin-converting enzyme 2;
EC=3.4.17.23;
AltName: Full=ACE-related carboxypeptidase;
AltName: Full=Angiotensin-converting enzyme homolog;
Short=ACEH;
AltName: Full=Metalloprotease MPROT15;
Contains:
RecName: Full=Processed angiotensin-converting enzyme 2;
Flags: Precursor;
Name=ACE2; ORFNames=UNQ868/PRO1885;
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), TISSUE SPECIFICITY, FUNCTION,
AND ENZYME REGULATION.
TISSUE=Heart;
PubMed=10969042; DOI=10.1161/01.RES.87.5.e1;
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M.,
Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R.,
Breitbart R.E., Acton S.;
"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2)
converts angiotensin I to angiotensin 1-9.";
Circ. Res. 87:E1-E9(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
GLYCOSYLATION, FUNCTION, AND ENZYME REGULATION.
TISSUE=Lymphoma;
PubMed=10924499; DOI=10.1074/jbc.M002615200;
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G.,
Turner A.J.;
"A human homolog of angiotensin-converting enzyme. Cloning and
functional expression as a captopril-insensitive carboxypeptidase.";
J. Biol. Chem. 275:33238-33243(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND ENZYME REGULATION.
TISSUE=Testis;
PubMed=15231706; DOI=10.1210/en.2004-0443;
Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A.,
Smith A.I., Lew R.A.;
"The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is
selectively expressed by adult Leydig cells of the testis.";
Endocrinology 145:4703-4711(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-638.
TISSUE=Lung, and Testis;
PubMed=15937940; DOI=10.1002/ajmg.a.30779;
Itoyama S., Keicho N., Hijikata M., Quy T., Phi N.C., Long H.T.,
Ha L.D., Ban V.V., Matsushita I., Yanai H., Kirikae F., Kirikae T.,
Kuratsuji T., Sasazuki T.;
"Identification of an alternative 5'-untranslated exon and new
polymorphisms of angiotensin-converting enzyme 2 gene: lack of
association with SARS in the Vietnamese population.";
Am. J. Med. Genet. A 136:52-57(2005).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Suzuki Y., Watanabe M., Sugano S.;
"Cloning, expression analysis and chromosomal localization of a novel
ACE like enzyme.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Southan C., Burgess N.;
"MPROT15 polypeptide and MPROT15 polynucleotide.";
Patent number CA2248987, 13-NOV-1999.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
Li K.K.B., Yip C.W., Hon C.C., Lam C.Y., Leung F.C.C.;
"Comparative susceptibility to SARS-CoV mediated by ACE2 protein of 15
different species.";
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-26.
SeattleSNPs variation discovery resource;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
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 [LARGE SCALE MRNA] OF 2-805 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[13]
PROTEIN SEQUENCE OF 679-689, IDENTIFICATION BY MASS SPECTROMETRY, AND
INTERACTION WITH ITGB1.
PubMed=15276642; DOI=10.1016/j.bbadis.2004.05.005;
Lin Q., Keller R.S., Weaver B., Zisman L.S.;
"Interaction of ACE2 and integrin beta1 in failing human heart.";
Biochim. Biophys. Acta 1689:175-178(2004).
[14]
TISSUE SPECIFICITY.
PubMed=12459472; DOI=10.1016/S0014-5793(02)03640-2;
Harmer D., Gilbert M., Borman R., Clark K.L.;
"Quantitative mRNA expression profiling of ACE 2, a novel homologue of
angiotensin converting enzyme.";
FEBS Lett. 532:107-110(2002).
[15]
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND COFACTOR.
PubMed=11815627; DOI=10.1074/jbc.M200581200;
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J.,
Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A.,
Nichols A., Tummino P.;
"Hydrolysis of biological peptides by human angiotensin-converting
enzyme-related carboxypeptidase.";
J. Biol. Chem. 277:14838-14843(2002).
[16]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE
GLYCOPROTEIN, GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14647384; DOI=10.1038/nature02145;
Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A.,
Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H.,
Farzan M.;
"Angiotensin-converting enzyme 2 is a functional receptor for the SARS
coronavirus.";
Nature 426:450-454(2003).
[17]
INDUCTION.
PubMed=15151696; DOI=10.1186/1741-7015-2-19;
Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.;
"ACE2 gene expression is up-regulated in the human failing heart.";
BMC Med. 2:19-19(2004).
[18]
TISSUE SPECIFICITY.
PubMed=15141377; DOI=10.1002/path.1570;
Hamming I., Timens W., Bulthuis M.L.C., Lely A.T., Navis G.J.,
van Goor H.;
"Tissue distribution of ACE2 protein, the functional receptor for SARS
coronavirus. A first step in understanding SARS pathogenesis.";
J. Pathol. 203:631-637(2004).
[19]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SARS-COV SPIKE
GLYCOPROTEIN.
PubMed=15452268; DOI=10.1128/JVI.78.20.11429-11433.2004;
Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M.,
Sullivan J.L., Farzan M., Choe H.;
"Efficient replication of severe acute respiratory syndrome
coronavirus in mouse cells is limited by murine angiotensin-converting
enzyme 2.";
J. Virol. 78:11429-11433(2004).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[21]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15671045; DOI=10.1093/eurheartj/ehi114;
Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S.,
Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E.,
Johnston C.I.;
"Myocardial infarction increases ACE2 expression in rat and humans.";
Eur. Heart J. 26:369-375(2005).
[22]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE
GLYCOPROTEIN, AND MUTAGENESIS.
PubMed=15791205; DOI=10.1038/sj.emboj.7600640;
Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K.,
Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A.,
Guan Y., Choe H., Farzan M.;
"Receptor and viral determinants of SARS-coronavirus adaptation to
human ACE2.";
EMBO J. 24:1634-1643(2005).
[23]
PROTEOLYTIC CLEAVAGE.
PubMed=15983030; DOI=10.1074/jbc.M505111200;
Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T.,
Smith A.I., Hooper N.M., Turner A.J.;
"Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated
ectodomain shedding of the severe-acute respiratory syndrome-
coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2
(ACE2).";
J. Biol. Chem. 280:30113-30119(2005).
[24]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HCOV-NL63 SPIKE
GLYCOPROTEIN.
PubMed=15897467; DOI=10.1073/pnas.0409465102;
Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B.,
Poehlmann S.;
"Human coronavirus NL63 employs the severe acute respiratory syndrome
coronavirus receptor for cellular entry.";
Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
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).
[26]
PROTEOLYTIC CLEAVAGE.
PubMed=21563828; DOI=10.1021/bi200525y;
Lai Z.W., Hanchapola I., Steer D.L., Smith A.I.;
"Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site
identification: determinants and constraints.";
Biochemistry 50:5182-5194(2011).
[27]
SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND INTERACTION WITH
TMPRSS2.
PubMed=21068237; DOI=10.1128/JVI.02062-10;
Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S.,
Gallagher T.;
"A transmembrane serine protease is linked to the severe acute
respiratory syndrome coronavirus receptor and activates virus entry.";
J. Virol. 85:873-882(2011).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
PubMed=24227843; DOI=10.1128/JVI.02202-13;
Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O.,
Poehlmann S.;
"TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by
TMPRSS2 augments entry driven by the severe acute respiratory syndrome
coronavirus spike protein.";
J. Virol. 88:1293-1307(2014).
[29]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-615, X-RAY CRYSTALLOGRAPHY
(3.0 ANGSTROMS) OF 19-615 IN COMPLEX WITH MLN-4760, DISULFIDE BONDS,
AND GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND
ASN-546.
PubMed=14754895; DOI=10.1074/jbc.M311191200;
Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T.,
Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A.,
Pantoliano M.W.;
"ACE2 X-ray structures reveal a large hinge-bending motion important
for inhibitor binding and catalysis.";
J. Biol. Chem. 279:17996-18007(2004).
-!- FUNCTION: Carboxypeptidase which converts angiotensin I to
angiotensin 1-9, a peptide of unknown function, and angiotensin II
to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-
13 and dynorphin-13 with high efficiency. May be an important
regulator of heart function. {ECO:0000269|PubMed:10924499,
ECO:0000269|PubMed:10969042, ECO:0000269|PubMed:14647384,
ECO:0000269|PubMed:24227843}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for SARS
coronavirus/SARS-CoV and human coronavirus NL63/HCoV-NL63.
{ECO:0000269|PubMed:14647384, ECO:0000269|PubMed:15452268,
ECO:0000269|PubMed:15791205, ECO:0000269|PubMed:15897467}.
-!- CATALYTIC ACTIVITY: Angiotensin II + H(2)O = angiotensin-(1-7) +
L-phenylalanine.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11815627};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11815627};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996;
Evidence={ECO:0000269|PubMed:11815627};
Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:11815627};
-!- ENZYME REGULATION: Activated by chloride and fluoride, but not
bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the
ACE inhibitors linosipril, captopril and enalaprilat.
{ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042,
ECO:0000269|PubMed:11815627, ECO:0000269|PubMed:15231706}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.9 uM for angiotensin I {ECO:0000269|PubMed:11815627};
KM=2 uM for angiotensin II {ECO:0000269|PubMed:11815627};
KM=6.8 uM for apelin-13 {ECO:0000269|PubMed:11815627};
KM=5.5 uM for dynorphin-13 {ECO:0000269|PubMed:11815627};
pH dependence:
Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6
to 9. {ECO:0000269|PubMed:11815627};
-!- SUBUNIT: Interacts with ITGB1. Interacts with the catalytically
active form of TMPRSS2. {ECO:0000269|PubMed:14754895,
ECO:0000269|PubMed:15276642, ECO:0000269|PubMed:21068237}.
-!- SUBUNIT: (Microbial infection) Interacts with SARS
coronavirus/SARS-CoV and human coronavirus NL63/HCoV-NL63 spike
glycoprotein (PubMed:14647384, PubMed:15452268, PubMed:15791205,
PubMed:15897467). {ECO:0000269|PubMed:14647384,
ECO:0000269|PubMed:15452268, ECO:0000269|PubMed:15791205,
ECO:0000269|PubMed:15897467}.
-!- INTERACTION:
Q6Q1S2:S (xeno); NbExp=3; IntAct=EBI-15814450, EBI-15814420;
-!- SUBCELLULAR LOCATION: Processed angiotensin-converting enzyme 2:
Secreted.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cytoplasm {ECO:0000250}. Note=Detected in both cell
membrane and cytoplasm in neurons. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BYF1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYF1-2; Sequence=VSP_014901, VSP_014902;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in endothelial cells from small and
large arteries, and in arterial smooth muscle cells. Expressed in
lung alveolar epithelial cells, enterocytes of the small
intestine, Leydig cells and Sertoli cells (at protein level).
Expressed in heart, kidney, testis, and gastrointestinal system.
{ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:10969042,
ECO:0000269|PubMed:12459472, ECO:0000269|PubMed:15141377,
ECO:0000269|PubMed:15231706, ECO:0000269|PubMed:15671045}.
-!- INDUCTION: Up-regulated in failing heart.
{ECO:0000269|PubMed:15151696, ECO:0000269|PubMed:15671045}.
-!- PTM: N-glycosylation on Asn-90 may limit SARS infectivity.
{ECO:0000269|PubMed:10924499, ECO:0000269|PubMed:14647384,
ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:19159218}.
-!- PTM: Proteolytic cleavage by ADAM17 generates a secreted form.
Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and
HPN/TMPRSS1. {ECO:0000269|PubMed:15983030,
ECO:0000269|PubMed:21068237, ECO:0000269|PubMed:21563828,
ECO:0000269|PubMed:24227843}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ace2/";
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EMBL; AF291820; AAF99721.1; -; mRNA.
EMBL; AF241254; AAF78220.1; -; mRNA.
EMBL; AY623811; AAT45083.1; -; mRNA.
EMBL; AB193259; BAD99266.1; -; mRNA.
EMBL; AB193260; BAD99267.1; -; mRNA.
EMBL; AB046569; BAB40370.1; -; mRNA.
EMBL; E39033; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; GQ262784; ACT66268.1; -; mRNA.
EMBL; AY358714; AAQ89076.1; -; mRNA.
EMBL; AY217547; AAO25651.1; -; Genomic_DNA.
EMBL; CH471074; EAW98892.1; -; Genomic_DNA.
EMBL; BC039902; AAH39902.1; -; mRNA.
EMBL; BC048094; AAH48094.2; -; mRNA.
EMBL; AL110224; CAB53682.1; -; mRNA.
CCDS; CCDS14169.1; -. [Q9BYF1-1]
PIR; T14762; T14762.
RefSeq; NP_068576.1; NM_021804.2. [Q9BYF1-1]
UniGene; Hs.178098; -.
PDB; 1R42; X-ray; 2.20 A; A=1-615.
PDB; 1R4L; X-ray; 3.00 A; A=1-615.
PDB; 1XJP; Model; -; B=19-615.
PDB; 2AJF; X-ray; 2.90 A; A/B=19-615.
PDB; 3D0G; X-ray; 2.80 A; A/B=56-615.
PDB; 3D0H; X-ray; 3.10 A; A/B=56-615.
PDB; 3D0I; X-ray; 2.90 A; A/B=56-615.
PDB; 3KBH; X-ray; 3.31 A; A/B/C/D=19-615.
PDB; 3SCI; X-ray; 2.90 A; A/B=19-615.
PDB; 3SCJ; X-ray; 3.00 A; A/B=19-615.
PDB; 3SCK; X-ray; 3.00 A; A/B=83-615.
PDB; 3SCL; X-ray; 3.00 A; A/B=83-615.
PDBsum; 1R42; -.
PDBsum; 1R4L; -.
PDBsum; 1XJP; -.
PDBsum; 2AJF; -.
PDBsum; 3D0G; -.
PDBsum; 3D0H; -.
PDBsum; 3D0I; -.
PDBsum; 3KBH; -.
PDBsum; 3SCI; -.
PDBsum; 3SCJ; -.
PDBsum; 3SCK; -.
PDBsum; 3SCL; -.
ProteinModelPortal; Q9BYF1; -.
SMR; Q9BYF1; -.
BioGrid; 121864; 6.
DIP; DIP-44689N; -.
IntAct; Q9BYF1; 3.
MINT; MINT-4538816; -.
STRING; 9606.ENSP00000252519; -.
BindingDB; Q9BYF1; -.
ChEMBL; CHEMBL3736; -.
DrugBank; DB00722; Lisinopril.
DrugBank; DB00691; Moexipril.
DrugBank; DB05203; SPP1148.
DrugBank; DB05358; TAK-491.
GuidetoPHARMACOLOGY; 1614; -.
MEROPS; M02.006; -.
iPTMnet; Q9BYF1; -.
PhosphoSitePlus; Q9BYF1; -.
BioMuta; ACE2; -.
DMDM; 71658783; -.
EPD; Q9BYF1; -.
PaxDb; Q9BYF1; -.
PeptideAtlas; Q9BYF1; -.
PRIDE; Q9BYF1; -.
Ensembl; ENST00000252519; ENSP00000252519; ENSG00000130234. [Q9BYF1-1]
Ensembl; ENST00000427411; ENSP00000389326; ENSG00000130234. [Q9BYF1-1]
GeneID; 59272; -.
KEGG; hsa:59272; -.
UCSC; uc004cxa.2; human. [Q9BYF1-1]
CTD; 59272; -.
DisGeNET; 59272; -.
EuPathDB; HostDB:ENSG00000130234.10; -.
GeneCards; ACE2; -.
HGNC; HGNC:13557; ACE2.
HPA; CAB026174; -.
HPA; HPA000288; -.
MIM; 300335; gene.
neXtProt; NX_Q9BYF1; -.
OpenTargets; ENSG00000130234; -.
PharmGKB; PA425; -.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
GeneTree; ENSGT00520000055576; -.
HOGENOM; HOG000292210; -.
HOVERGEN; HBG000265; -.
InParanoid; Q9BYF1; -.
KO; K09708; -.
OMA; DFLTAHH; -.
OrthoDB; EOG091G033S; -.
PhylomeDB; Q9BYF1; -.
TreeFam; TF312861; -.
BRENDA; 3.4.15.1; 2681.
BRENDA; 3.4.17.23; 2681.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
SABIO-RK; Q9BYF1; -.
ChiTaRS; ACE2; human.
EvolutionaryTrace; Q9BYF1; -.
GeneWiki; Angiotensin-converting_enzyme_2; -.
GenomeRNAi; 59272; -.
PMAP-CutDB; Q9BYF1; -.
PRO; PR:Q9BYF1; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000130234; -.
CleanEx; HS_ACE2; -.
Genevisible; Q9BYF1; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; TAS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004180; F:carboxypeptidase activity; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0004181; F:metallocarboxypeptidase activity; EXP:Reactome.
GO; GO:0001618; F:virus receptor activity; IDA:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; TAS:BHF-UCL.
GO; GO:0002005; P:angiotensin catabolic process in blood; IC:BHF-UCL.
GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
GO; GO:0003051; P:angiotensin-mediated drinking behavior; IMP:BHF-UCL.
GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Ensembl.
GO; GO:1903598; P:positive regulation of gap junction assembly; IMP:BHF-UCL.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IC:BHF-UCL.
GO; GO:0032800; P:receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL.
GO; GO:0097746; P:regulation of blood vessel diameter; IC:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; IMP:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; TAS:BHF-UCL.
GO; GO:0001817; P:regulation of cytokine production; IC:BHF-UCL.
GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IMP:BHF-UCL.
GO; GO:0019229; P:regulation of vasoconstriction; IC:BHF-UCL.
GO; GO:0015827; P:tryptophan transport; IEA:Ensembl.
GO; GO:0046718; P:viral entry into host cell; TAS:UniProtKB.
CDD; cd06461; M2_ACE; 1.
Gene3D; 1.20.5.100; -; 1.
InterPro; IPR031588; Collectrin_dom.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 1.
Pfam; PF16959; Collectrin; 1.
Pfam; PF01401; Peptidase_M2; 1.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane;
Chloride; Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Polymorphism; Protease; Receptor; Reference proteome;
Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 805 Angiotensin-converting enzyme 2.
/FTId=PRO_0000028570.
CHAIN 18 708 Processed angiotensin-converting enzyme
2.
/FTId=PRO_0000292268.
TOPO_DOM 18 740 Extracellular. {ECO:0000255}.
TRANSMEM 741 761 Helical. {ECO:0000255}.
TOPO_DOM 762 805 Cytoplasmic. {ECO:0000255}.
REGION 30 41 Interaction with SARS-CoV spike
glycoprotein.
REGION 82 84 Interaction with SARS-CoV spike
glycoprotein.
REGION 353 357 Interaction with SARS-CoV spike
glycoprotein.
REGION 652 659 Essential for cleavage by ADAM17.
REGION 697 716 Essential for cleavage by TMPRSS11D and
TMPRSS2.
ACT_SITE 375 375
ACT_SITE 505 505
METAL 374 374 Zinc; catalytic.
METAL 378 378 Zinc; catalytic.
METAL 402 402 Zinc; catalytic.
BINDING 169 169 Chloride.
BINDING 273 273 Substrate.
BINDING 345 345 Substrate.
BINDING 346 346 Substrate; via carbonyl oxygen.
BINDING 371 371 Substrate.
BINDING 477 477 Chloride.
BINDING 481 481 Chloride.
BINDING 515 515 Substrate.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:14754895}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14754895,
ECO:0000269|PubMed:15084671}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14754895}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:14754895}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14754895}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14754895,
ECO:0000269|PubMed:19159218}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 133 141 {ECO:0000269|PubMed:14754895}.
DISULFID 344 361 {ECO:0000269|PubMed:14754895}.
DISULFID 530 542 {ECO:0000269|PubMed:14754895}.
VAR_SEQ 555 555 F -> L (in isoform 2).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_014901.
VAR_SEQ 556 805 Missing (in isoform 2).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_014902.
VARIANT 26 26 K -> R (in dbSNP:rs4646116).
{ECO:0000269|Ref.9}.
/FTId=VAR_023082.
VARIANT 638 638 N -> S (in dbSNP:rs183135788).
{ECO:0000269|PubMed:15937940}.
/FTId=VAR_023083.
MUTAGEN 24 26 QAK->KAE: Slightly inhibits interaction
with SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 31 31 K->D: Abolishes interaction with SARS-CoV
spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 37 37 E->A: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 38 38 D->A: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 41 41 Y->A: Strongly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 68 68 K->D: Slightly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 82 84 MYP->NFS: Inhibits interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 110 110 E->P: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 135 136 PD->SM: No effect on interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 160 160 E->R: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 192 192 R->D: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 219 219 R->D: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 239 239 H->Q: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 309 309 K->D: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 312 312 E->A: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 324 324 T->A: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 338 340 NVQ->DDR: No effect on interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 350 350 D->A: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 353 353 K->H,A,D: Abolishes interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 355 355 D->A: Strongly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 357 357 R->A: Strongly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 359 359 L->K,A: No effect on interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 383 383 M->A: Slightly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 389 389 P->A: Slightly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 393 393 R->A: Slightly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 425 427 SPD->PSN: Slightly inhibits interaction
with SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 465 467 KGE->QDK: No effect on interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 559 559 R->S: Slightly inhibits interaction with
SARS-CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
MUTAGEN 603 603 F->T: No effect on interaction with SARS-
CoV spike glycoprotein.
{ECO:0000269|PubMed:15791205}.
CONFLICT 18 18 Q -> H (in Ref. 12; CAB53682).
{ECO:0000305}.
CONFLICT 508 508 N -> D (in Ref. 8; AAQ89076).
{ECO:0000305}.
CONFLICT 631 631 K -> R (in Ref. 5; BAB40370).
{ECO:0000305}.
HELIX 23 52 {ECO:0000244|PDB:1R42}.
HELIX 56 77 {ECO:0000244|PDB:1R42}.
TURN 78 82 {ECO:0000244|PDB:1R42}.
HELIX 85 87 {ECO:0000244|PDB:3D0G}.
HELIX 91 100 {ECO:0000244|PDB:1R42}.
HELIX 104 107 {ECO:0000244|PDB:1R42}.
HELIX 110 129 {ECO:0000244|PDB:1R42}.
STRAND 131 134 {ECO:0000244|PDB:1R42}.
STRAND 137 143 {ECO:0000244|PDB:1R42}.
TURN 144 146 {ECO:0000244|PDB:1R42}.
HELIX 148 154 {ECO:0000244|PDB:1R42}.
HELIX 158 171 {ECO:0000244|PDB:1R42}.
HELIX 173 193 {ECO:0000244|PDB:1R42}.
STRAND 196 198 {ECO:0000244|PDB:1R4L}.
HELIX 199 204 {ECO:0000244|PDB:1R42}.
TURN 205 207 {ECO:0000244|PDB:1R42}.
TURN 213 215 {ECO:0000244|PDB:1R42}.
HELIX 220 251 {ECO:0000244|PDB:1R42}.
TURN 253 255 {ECO:0000244|PDB:1R42}.
STRAND 258 260 {ECO:0000244|PDB:3SCJ}.
HELIX 264 266 {ECO:0000244|PDB:1R42}.
STRAND 267 271 {ECO:0000244|PDB:1R42}.
HELIX 276 278 {ECO:0000244|PDB:1R42}.
HELIX 279 282 {ECO:0000244|PDB:1R42}.
TURN 284 287 {ECO:0000244|PDB:1R42}.
TURN 294 297 {ECO:0000244|PDB:1R42}.
HELIX 298 300 {ECO:0000244|PDB:1R42}.
HELIX 304 316 {ECO:0000244|PDB:1R42}.
TURN 317 319 {ECO:0000244|PDB:1R42}.
HELIX 327 330 {ECO:0000244|PDB:1R42}.
STRAND 338 340 {ECO:0000244|PDB:3D0G}.
STRAND 347 352 {ECO:0000244|PDB:1R42}.
STRAND 355 359 {ECO:0000244|PDB:1R42}.
HELIX 366 384 {ECO:0000244|PDB:1R42}.
TURN 385 387 {ECO:0000244|PDB:1R42}.
HELIX 390 392 {ECO:0000244|PDB:1R42}.
HELIX 400 413 {ECO:0000244|PDB:1R42}.
HELIX 415 420 {ECO:0000244|PDB:1R42}.
TURN 422 426 {ECO:0000244|PDB:1R4L}.
HELIX 432 446 {ECO:0000244|PDB:1R42}.
HELIX 449 465 {ECO:0000244|PDB:1R42}.
STRAND 466 468 {ECO:0000244|PDB:1R4L}.
HELIX 470 472 {ECO:0000244|PDB:1R42}.
HELIX 473 483 {ECO:0000244|PDB:1R42}.
STRAND 486 488 {ECO:0000244|PDB:3D0G}.
HELIX 499 502 {ECO:0000244|PDB:1R42}.
HELIX 504 507 {ECO:0000244|PDB:1R42}.
HELIX 514 531 {ECO:0000244|PDB:1R42}.
TURN 532 534 {ECO:0000244|PDB:1R42}.
HELIX 539 541 {ECO:0000244|PDB:1R42}.
HELIX 548 558 {ECO:0000244|PDB:1R42}.
TURN 559 562 {ECO:0000244|PDB:1R42}.
HELIX 566 574 {ECO:0000244|PDB:1R42}.
STRAND 575 578 {ECO:0000244|PDB:1R42}.
HELIX 582 598 {ECO:0000244|PDB:1R42}.
STRAND 600 602 {ECO:0000244|PDB:1R42}.
STRAND 607 609 {ECO:0000244|PDB:1R42}.
SEQUENCE 805 AA; 92463 MW; 8EE6EB0A931550E8 CRC64;
MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY NTNITEENVQ
NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL QQNGSSVLSE DKSKRLNTIL
NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE IMANSLDYNE RLWAWESWRS EVGKQLRPLY
EEYVVLKNEM ARANHYEDYG DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL
HAYVRAKLMN AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ
AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD LGKGDFRILM
CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF HEAVGEIMSL SAATPKHLKS
IGLLSPDFQE DNETEINFLL KQALTIVGTL PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM
KREIVGVVEP VPHDETYCDP ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH
KCDISNSTEA GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK
NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA MRQYFLKVKN
QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV EKAIRMSRSR INDAFRLNDN
SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM GVIVVGIVIL IFTGIRDRKK KNKARSGENP
YASIDISKGE NNPGFQNTDD VQTSF


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