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Angiotensin-converting enzyme (ACE) (EC 3.2.1.-) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) (CD antigen CD143) [Cleaved into: Angiotensin-converting enzyme, soluble form]

 ACE_MOUSE               Reviewed;        1312 AA.
P09470; P22967; Q6GTS2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 3.
25-OCT-2017, entry version 171.
RecName: Full=Angiotensin-converting enzyme;
Short=ACE;
EC=3.2.1.-;
EC=3.4.15.1;
AltName: Full=Dipeptidyl carboxypeptidase I;
AltName: Full=Kininase II;
AltName: CD_antigen=CD143;
Contains:
RecName: Full=Angiotensin-converting enzyme, soluble form;
Flags: Precursor;
Name=Ace; Synonyms=Dcp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
PubMed=2545691;
Bernstein K.E., Martin B.M., Edwards A.S., Bernstein E.A.;
"Mouse angiotensin-converting enzyme is a protein composed of two
homologous domains.";
J. Biol. Chem. 264:11945-11951(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), AND PARTIAL
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2164636; DOI=10.1128/MCB.10.8.4294;
Howard T.E., Shai S.-Y., Langford K.G., Martin B.M., Bernstein K.E.;
"Transcription of testicular angiotensin-converting enzyme (ACE) is
initiated within the 12th intron of the somatic ACE gene.";
Mol. Cell. Biol. 10:4294-4302(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SOMATIC).
STRAIN=FVB/N; TISSUE=Mammary gland;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-332 (ISOFORM SOMATIC), AND PARTIAL
PROTEIN SEQUENCE.
PubMed=2841312;
Bernstein K.E., Martin B.M., Bernstein E.A., Linton J., Striker L.,
Striker G.;
"The isolation of angiotensin-converting enzyme cDNA.";
J. Biol. Chem. 263:11021-11024(1988).
[5]
PROTEIN SEQUENCE OF 35-54.
TISSUE=Kidney;
PubMed=2835538; DOI=10.1038/ki.1988.48;
Bernstein K.E., Martin B.M., Striker L., Striker G.;
"Partial protein sequence of mouse and bovine kidney angiotensin
converting enzyme.";
Kidney Int. 33:652-655(1988).
[6]
FUNCTION.
PubMed=7753170; DOI=10.1038/375146a0;
Krege J.H., John S.W., Langenbach L.L., Hodgin J.B., Hagaman J.R.,
Bachman E.S., Jennette J.C., O'Brien D.A., Smithies O.;
"Male-female differences in fertility and blood pressure in ACE-
deficient mice.";
Nature 375:146-148(1995).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8642790;
Esther C.R. Jr., Howard T.E., Marino E.M., Goddard J.M.,
Capecchi M.R., Bernstein K.E.;
"Mice lacking angiotensin-converting enzyme have low blood pressure,
renal pathology, and reduced male fertility.";
Lab. Invest. 74:953-965(1996).
[8]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF HIS-993; GLU-994 AND
HIS-997.
PubMed=15665832; DOI=10.1038/nm1179;
Kondoh G., Tojo H., Nakatani Y., Komazawa N., Murata C., Yamagata K.,
Maeda Y., Kinoshita T., Okabe M., Taguchi R., Takeda J.;
"Angiotensin-converting enzyme is a GPI-anchored protein releasing
factor crucial for fertilization.";
Nat. Med. 11:160-166(2005).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
SUBCELLULAR LOCATION.
PubMed=23535237; DOI=10.1152/ajpcell.00364.2012;
Xiao L., Haack K.K., Zucker I.H.;
"Angiotensin II regulates ACE and ACE2 in neurons through p38 mitogen-
activated protein kinase and extracellular signal-regulated kinase 1/2
signaling.";
Am. J. Physiol. 304:C1073-C1079(2013).
-!- FUNCTION: Converts angiotensin I to angiotensin II by release of
the terminal His-Leu, this results in an increase of the
vasoconstrictor activity of angiotensin. Also able to inactivate
bradykinin, a potent vasodilator. Has also a glycosidase activity
which releases GPI-anchored proteins from the membrane by cleaving
the mannose linkage in the GPI moiety. This GPIase activity seems
to be crucial for the egg-binding ability of the sperm.
{ECO:0000269|PubMed:15665832, ECO:0000269|PubMed:7753170,
ECO:0000269|PubMed:8642790}.
-!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither
Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II,
with increase in vasoconstrictor activity, but no action on
angiotensin II.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. Isoform Testis-specific only
binds 1 Zn(2+) ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
Note=Binds 3 chloride ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Peptidase activity is specifically inhibited by
lisinopril, captopril and enalaprilat. In contrast, GPIase
activity is nearly insensitive to captopril.
{ECO:0000269|PubMed:15665832}.
-!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
Secreted {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23535237};
Single-pass type I membrane protein {ECO:0000269|PubMed:23535237}.
Cytoplasm {ECO:0000269|PubMed:23535237}. Note=Detected in both
cell membrane and cytoplasm in neurons.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Somatic;
IsoId=P09470-1; Sequence=Displayed;
Name=Testis-specific; Synonyms=ACE-T;
IsoId=P09470-2, P22967-1;
Sequence=VSP_037638, VSP_037639;
-!- TISSUE SPECIFICITY: Testis-specific isoform is expressed in
spermatocytes, adult testis.
-!- INDUCTION: Expression is thought to be subject to hormonal
regulation by androgens.
-!- PTM: Phosphorylated by CK2 on Ser-1305; which allows membrane
retention. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Low blood pressure, elevated serum
potassium, anemia, and renal defects. Male mice have reduced
fertility. {ECO:0000269|PubMed:8642790}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
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EMBL; J04946; AAA37147.1; -; mRNA.
EMBL; J04947; AAA37148.1; -; mRNA.
EMBL; M55333; AAA37149.1; -; mRNA.
EMBL; M61094; AAA37150.1; -; Genomic_DNA.
EMBL; BC040404; AAH40404.1; -; mRNA.
EMBL; J03940; AAA37146.1; -; mRNA.
CCDS; CCDS25543.1; -. [P09470-1]
CCDS; CCDS25544.1; -. [P09470-2]
PIR; A34171; A34171.
PIR; A35655; A35655.
RefSeq; NP_033728.1; NM_009598.2. [P09470-2]
RefSeq; NP_997507.1; NM_207624.5. [P09470-1]
UniGene; Mm.754; -.
ProteinModelPortal; P09470; -.
SMR; P09470; -.
BioGrid; 197920; 1.
IntAct; P09470; 3.
MINT; MINT-4086662; -.
STRING; 10090.ENSMUSP00000001963; -.
BindingDB; P09470; -.
ChEMBL; CHEMBL2994; -.
MEROPS; M02.001; -.
iPTMnet; P09470; -.
PhosphoSitePlus; P09470; -.
PaxDb; P09470; -.
PeptideAtlas; P09470; -.
PRIDE; P09470; -.
Ensembl; ENSMUST00000001963; ENSMUSP00000001963; ENSMUSG00000020681. [P09470-1]
Ensembl; ENSMUST00000001964; ENSMUSP00000001964; ENSMUSG00000020681. [P09470-2]
GeneID; 11421; -.
KEGG; mmu:11421; -.
UCSC; uc007lxu.2; mouse. [P09470-1]
UCSC; uc007lxw.2; mouse. [P09470-2]
CTD; 1636; -.
MGI; MGI:87874; Ace.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
GeneTree; ENSGT00520000055576; -.
HOGENOM; HOG000007838; -.
HOVERGEN; HBG000264; -.
InParanoid; P09470; -.
KO; K01283; -.
OMA; VTMEQLF; -.
OrthoDB; EOG091G033S; -.
PhylomeDB; P09470; -.
TreeFam; TF312861; -.
Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
PRO; PR:P09470; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020681; -.
ExpressionAtlas; P09470; baseline and differential.
Genevisible; P09470; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0031711; F:bradykinin receptor binding; ISO:MGI.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031404; F:chloride ion binding; ISO:MGI.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
GO; GO:0008238; F:exopeptidase activity; ISO:MGI.
GO; GO:0070573; F:metallodipeptidase activity; ISO:MGI.
GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IMP:MGI.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:UniProtKB.
GO; GO:0008240; F:tripeptidyl-peptidase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0050435; P:amyloid-beta metabolic process; ISO:MGI.
GO; GO:0050482; P:arachidonic acid secretion; ISO:MGI.
GO; GO:0071838; P:cell proliferation in bone marrow; IMP:BHF-UCL.
GO; GO:0060047; P:heart contraction; IMP:MGI.
GO; GO:0042447; P:hormone catabolic process; IDA:BHF-UCL.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:1903597; P:negative regulation of gap junction assembly; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IMP:BHF-UCL.
GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
GO; GO:0043171; P:peptide catabolic process; ISO:MGI.
GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; IMP:BHF-UCL.
GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IMP:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IMP:BHF-UCL.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:BHF-UCL.
GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; IMP:BHF-UCL.
GO; GO:0060177; P:regulation of angiotensin metabolic process; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; IDA:BHF-UCL.
GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IMP:BHF-UCL.
GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISO:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
CDD; cd06461; M2_ACE; 2.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 2.
Pfam; PF01401; Peptidase_M2; 2.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 2.
1: Evidence at protein level;
Alternative splicing; Carboxypeptidase; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 34 {ECO:0000269|PubMed:2835538}.
CHAIN 35 1312 Angiotensin-converting enzyme.
/FTId=PRO_0000028539.
CHAIN 35 1237 Angiotensin-converting enzyme, soluble
form.
/FTId=PRO_0000028540.
PROPEP 1238 1312 Removed in secreted form. {ECO:0000250}.
/FTId=PRO_0000028541.
TOPO_DOM 35 1264 Extracellular. {ECO:0000255}.
TRANSMEM 1265 1281 Helical. {ECO:0000255}.
TOPO_DOM 1282 1312 Cytoplasmic. {ECO:0000255}.
REGION 35 635 Peptidase M2 1.
REGION 636 1237 Peptidase M2 2.
ACT_SITE 396 396 1. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
ACT_SITE 994 994 2.
METAL 395 395 Zinc 1; catalytic. {ECO:0000250}.
METAL 399 399 Zinc 1; catalytic. {ECO:0000250}.
METAL 423 423 Zinc 1; catalytic. {ECO:0000250}.
METAL 993 993 Zinc 2; catalytic.
METAL 997 997 Zinc 2; catalytic.
METAL 1021 1021 Zinc 2; catalytic. {ECO:0000250}.
BINDING 236 236 Chloride 1. {ECO:0000250}.
BINDING 534 534 Chloride 1. {ECO:0000250}.
BINDING 796 796 Chloride 2. {ECO:0000250}.
BINDING 834 834 Chloride 3. {ECO:0000250}.
BINDING 1095 1095 Chloride 2. {ECO:0000250}.
BINDING 1099 1099 Chloride 2. {ECO:0000250}.
BINDING 1132 1132 Chloride 3. {ECO:0000250}.
MOD_RES 1305 1305 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 514 514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 682 682 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 700 700 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000250}.
CARBOHYD 719 719 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000250}.
CARBOHYD 765 765 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 947 947 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1196 1196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 162 170 {ECO:0000250}.
DISULFID 762 768 {ECO:0000250}.
DISULFID 962 980 {ECO:0000250}.
DISULFID 1148 1160 {ECO:0000250}.
VAR_SEQ 1 580 Missing (in isoform Testis-specific).
{ECO:0000303|PubMed:2164636}.
/FTId=VSP_037638.
VAR_SEQ 581 646 GCSRPWQEVLKDLVGSDALDAKALLEYFQPVSQWLEEQNQR
NGEVLGWPENQWRPPLPDNYPEGID -> MGQGWATPGLPS
FLFLLLCCGHHLLVLSQVATDHVTANQGITNQATTRSQTTT
HQATIDQTTQIPN (in isoform Testis-
specific). {ECO:0000303|PubMed:2164636}.
/FTId=VSP_037639.
MUTAGEN 993 993 H->K: Abolishes peptidase activity but no
effect on GPIase activity; when
associated with K-997.
{ECO:0000269|PubMed:15665832}.
MUTAGEN 994 994 E->D: Abolishes peptidase activity but no
effect on GPIase activity.
{ECO:0000269|PubMed:15665832}.
MUTAGEN 997 997 H->K: Abolishes peptidase activity but no
effect on GPIase activity; when
associated with K-993.
{ECO:0000269|PubMed:15665832}.
CONFLICT 568 568 A -> T (in Ref. 1; AAA37147).
{ECO:0000305}.
SEQUENCE 1312 AA; 150918 MW; 7DF9F5BE91762DFF CRC64;
MGAASGQRGR WPLSPPLLML SLLVLLLQPS PAPALDPGLQ PGNFSPDEAG AQLFAESYNS
SAEVVMFQST VASWAHDTNI TEENARRQEE AALVSQEFAE VWGKKAKELY ESIWQNFTDS
KLRRIIGSIR TLGPANLPLA QRQQYNSLLS NMSRIYSTGK VCFPNKTATC WSLDPELTNI
LASSRSYAKL LFAWEGWHDA VGIPLKPLYQ DFTAISNEAY RQDDFSDTGA FWRSWYESPS
FEESLEHIYH QLEPLYLNLH AYVRRALHRR YGDKYVNLRG PIPAHLLGDM WAQSWENIYD
MVVPFPDKPN LDVTSTMVQK GWNATHMFRV SEEFFTSLGL SPMPPEFWAE SMLEKPTDGR
EVVCHASAWD FYNRKDFRIK QCTRVTMEQL ATVHHEMGHV QYYLQYKDLH VSLRRGANPG
FHEAIGDVLA LSVSTPAHLH KIGLLDHVTN DIESDINYLL KMALEKIAFL PFGYLVDQWR
WGVFSGRTPP SRYNFDWWYL RTKYQGICPP VARNETHFDA GAKFHIPNVT PYIRYFVSFV
LQFQFHQALC KEAGHQGPLH QCDIYQSAQA GAKLKQVLQA GCSRPWQEVL KDLVGSDALD
AKALLEYFQP VSQWLEEQNQ RNGEVLGWPE NQWRPPLPDN YPEGIDLETD EAKADRFVEE
YDRTAQVLLN EYAEANWQYN TNITIEGSKI LLEKSTEVSN HTLKYGTRAK TFDVSNFQNS
SIKRIIKKLQ NLDRAVLPPK ELEEYNQILL DMETTYSLSN ICYTNGTCMP LEPDLTNMMA
TSRKYEELLW AWKSWRDKVG RAILPFFPKY VEFSNKIAKL NGYTDAGDSW RSLYESDNLE
QDLEKLYQEL QPLYLNLHAY VRRSLHRHYG SEYINLDGPI PAHLLGNMWA QTWSNIYDLV
APFPSAPNID ATEAMIKQGW TPRRIFKEAD NFFTSLGLLP VPPEFWNKSM LEKPTDGREV
VCHPSAWDFY NGKDFRIKQC TSVNMEDLVI AHHEMGHIQY FMQYKDLPVT FREGANPGFH
EAIGDIMALS VSTPKHLYSL NLLSTEGSGY EYDINFLMKM ALDKIAFIPF SYLIDQWRWR
VFDGSITKEN YNQEWWSLRL KYQGLCPPVP RSQGDFDPGS KFHVPANVPY VRYFVSFIIQ
FQFHEALCRA AGHTGPLHKC DIYQSKEAGK LLADAMKLGY SKPWPEAMKL ITGQPNMSAS
AMMNYFKPLT EWLVTENRRH GETLGWPEYN WAPNTARAEG STAESNRVNF LGLYLEPQQA
RVGQWVLLFL GVALLVATVG LAHRLYNIRN HHSLRRPHRG PQFGSEVELR HS


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E0004r ELISA kit ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Rat,Rattus norvegicus 96T
E0004m ELISA kit ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
E0004b ELISA kit ACE,ACE,Angiotensin-converting enzyme,Bos taurus,Bovine,DCP1,Dipeptidyl carboxypeptidase I,Kininase II 96T
U0004m CLIA ACE,Ace,Angiotensin-converting enzyme,Dcp1,Dipeptidyl carboxypeptidase I,Kininase II,Mouse,Mus musculus 96T
E0004h ELISA kit ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
U0004h CLIA ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
E0004Rb ELISA kit ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
E0004Rb ELISA ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
U0004Rb CLIA ACE,ACE,Angiotensin-converting enzyme,DCP1,Dipeptidyl carboxypeptidase I,Kininase II,Oryctolagus cuniculus,Rabbit 96T
E0004h ELISA ACE,ACE,Angiotensin-converting enzyme,DCP,DCP1,Dipeptidyl carboxypeptidase I,Homo sapiens,Human,Kininase II 96T
U1886h CLIA kit ACE2,ACEH,ACE-related carboxypeptidase,Angiotensin-converting enzyme 2,Angiotensin-converting enzyme homolog,Homo sapiens,Human,Metalloprotease MPROT15,UNQ868_PRO1885 96T
E1886h ELISA kit ACE2,ACEH,ACE-related carboxypeptidase,Angiotensin-converting enzyme 2,Angiotensin-converting enzyme homolog,Homo sapiens,Human,Metalloprotease MPROT15,UNQ868_PRO1885 96T


 

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