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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_RABIT               Reviewed;        1310 AA.
P12822; O02852; P22968;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
16-JAN-2019, entry version 138.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
TISSUE=Lung;
PubMed=1311831; DOI=10.1093/nar/20.4.683;
Thekkumkara T.J., Livingston W. III, Kumar R.S., Sen G.C.;
"Use of alternative polyadenylation sites for tissue-specific
transcription of two angiotensin-converting enzyme mRNAs.";
Nucleic Acids Res. 20:683-687(1992).
[2]
SEQUENCE REVISION.
Sen G.C.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
STRAIN=New Zealand white; TISSUE=Testis;
PubMed=2550457;
Kumar R.S., Kusari J., Roy S.N., Soffer R.L., Sen G.C.;
"Structure of testicular angiotensin-converting enzyme. A segmental
mosaic isozyme.";
J. Biol. Chem. 264:16754-16758(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88, AND ALTERNATIVE SPLICING.
TISSUE=Liver;
PubMed=1847388;
Kumar R.S., Thekkumkara T.J., Sen G.C.;
"The mRNAs encoding the two angiotensin-converting isozymes are
transcribed from the same gene by a tissue-specific choice of
alternative transcription initiation sites.";
J. Biol. Chem. 266:3854-3862(1991).
[5]
PROTEIN SEQUENCE OF 34-44 AND 755-758.
PubMed=6291514; DOI=10.1016/0006-291X(82)90634-9;
Iwata K., Lai C.Y., El-Dorry H.A., Soffer R.L.;
"The NH2- and COOH-terminal sequences of the angiotensin-converting
enzyme isozymes from rabbit lung and testis.";
Biochem. Biophys. Res. Commun. 107:1097-1103(1982).
[6]
PROTEIN SEQUENCE OF 34-55.
TISSUE=Lung;
PubMed=6314908; DOI=10.1016/0003-9861(83)90362-4;
Iwata K., Blacher R., Soffer R.L., Lai C.Y.;
"Rabbit pulmonary angiotensin-converting enzyme: the NH2-terminal
fragment with enzymatic activity and its formation from the native
enzyme by NH4OH treatment.";
Arch. Biochem. Biophys. 227:188-201(1983).
[7]
PROTEIN SEQUENCE OF 34-55, AND GLYCOSYLATION.
PubMed=1654880; DOI=10.1042/bj2780375;
Kirley T.L.;
"The Mg(2+)-ATPase of rabbit skeletal-muscle transverse tubule is a
highly glycosylated multiple-subunit enzyme.";
Biochem. J. 278:375-380(1991).
[8]
NUCLEOTIDE SEQUENCE OF 646-746.
PubMed=1705622;
Sen G.C., Thekkumkara T.J., Kumar R.S.;
"Angiotensin-converting enzyme: structural relationship of the
testicular and the pulmonary forms.";
J. Cardiovasc. Pharmacol. 16:S14-S18(1990).
[9]
PROTEIN SEQUENCE OF 727-733 AND 809-815.
PubMed=2176870; DOI=10.1021/bi00498a011;
Chen Y.N., Riordan J.F.;
"Identification of essential tyrosine and lysine residues in
angiotensin converting enzyme: evidence for a single active site.";
Biochemistry 29:10493-10498(1990).
[10]
PROTEIN SEQUENCE OF 1237-1259, AND CLEAVAGE SITE.
PubMed=8294466;
Ramchandran R., Sen G.C., Misono K., Sen I.;
"Regulated cleavage-secretion of the membrane-bound angiotensin-
converting enzyme.";
J. Biol. Chem. 269:2125-2130(1994).
[11]
MUTAGENESIS OF LYS-727 AND TYR-809, ACTIVITY REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7902354;
Sen I., Kasturi S., Abdul-Jabbar M., Sen G.C.;
"Mutations in two specific residues of testicular angiotensin-
converting enzyme change its catalytic properties.";
J. Biol. Chem. 268:25748-25754(1993).
-!- 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 (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=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.;
EC=3.4.15.1;
-!- 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};
-!- ACTIVITY REGULATION: Strongly activated by chloride. Specifically
inhibited by lisinopril. {ECO:0000269|PubMed:7902354}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.6 mM for Hip-His-Leu {ECO:0000269|PubMed:7902354};
KM=0.09 mM for angiotensin I {ECO:0000269|PubMed:7902354};
-!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
Secreted {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
Note=Detected in both cell membrane and cytoplasm in neurons.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Somatic;
IsoId=P12822-1; Sequence=Displayed;
Name=Testis-specific; Synonyms=ACE-T;
IsoId=P12822-2, P22968-1;
Sequence=VSP_037644, VSP_037645;
-!- TISSUE SPECIFICITY: Testis-specific isoform is expressed in
spermatocytes, adult testis.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:1654880}.
-!- PTM: Phosphorylated by CK2 on Ser-1303; which allows membrane
retention. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X62551; CAA44428.1; -; mRNA.
EMBL; J05041; AAA31153.1; -; mRNA.
EMBL; M58579; AAA31151.1; ALT_SEQ; Genomic_DNA.
EMBL; M58580; AAA31152.1; -; Genomic_DNA.
PIR; A34402; A34402.
PIR; S35484; S35484.
RefSeq; NP_001075864.1; NM_001082395.1. [P12822-1]
RefSeq; NP_001164540.1; NM_001171069.1. [P12822-2]
UniGene; Ocu.1824; -.
ProteinModelPortal; P12822; -.
SMR; P12822; -.
STRING; 9986.ENSOCUP00000016378; -.
BindingDB; P12822; -.
ChEMBL; CHEMBL4074; -.
MEROPS; M02.001; -.
PRIDE; P12822; -.
GeneID; 100009274; -.
KEGG; ocu:100009274; -.
CTD; 1636; -.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
HOGENOM; HOG000007838; -.
HOVERGEN; HBG000264; -.
InParanoid; P12822; -.
KO; K01283; -.
OrthoDB; 422699at2759; -.
SABIO-RK; P12822; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
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 33 {ECO:0000269|PubMed:1654880,
ECO:0000269|PubMed:6291514,
ECO:0000269|PubMed:6314908}.
CHAIN 34 1310 Angiotensin-converting enzyme.
/FTId=PRO_0000028551.
CHAIN 34 1236 Angiotensin-converting enzyme, soluble
form.
/FTId=PRO_0000028552.
PROPEP 1237 1310 Removed in secreted form. {ECO:0000250}.
/FTId=PRO_0000028553.
TOPO_DOM 34 1260 Extracellular. {ECO:0000255}.
TRANSMEM 1261 1281 Helical. {ECO:0000255}.
TOPO_DOM 1282 1310 Cytoplasmic. {ECO:0000255}.
REGION 35 634 Peptidase M2 1.
REGION 635 1236 Peptidase M2 2.
ACT_SITE 396 396 1. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
ACT_SITE 993 993 2. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 395 395 Zinc 1; catalytic. {ECO:0000250}.
METAL 399 399 Zinc 1; catalytic. {ECO:0000250}.
METAL 422 422 Zinc 1; catalytic. {ECO:0000250}.
METAL 992 992 Zinc 2; catalytic. {ECO:0000250}.
METAL 996 996 Zinc 2; catalytic. {ECO:0000250}.
METAL 1020 1020 Zinc 2; catalytic. {ECO:0000250}.
BINDING 236 236 Chloride 1. {ECO:0000250}.
BINDING 533 533 Chloride 1. {ECO:0000250}.
BINDING 795 795 Chloride 2. {ECO:0000250}.
BINDING 833 833 Chloride 3. {ECO:0000250}.
BINDING 1094 1094 Chloride 2. {ECO:0000250}.
BINDING 1098 1098 Chloride 2. {ECO:0000250}.
BINDING 1131 1131 Chloride 3. {ECO:0000250}.
SITE 1237 1238 Cleavage.
MOD_RES 1303 1303 Phosphoserine.
{ECO:0000250|UniProtKB:P12821}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 681 681 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 718 718 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 946 946 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1195 1195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 162 170 {ECO:0000250}.
DISULFID 761 767 {ECO:0000250}.
DISULFID 961 979 {ECO:0000250}.
DISULFID 1147 1159 {ECO:0000250}.
VAR_SEQ 1 573 Missing (in isoform Testis-specific).
{ECO:0000303|PubMed:2550457}.
/FTId=VSP_037644.
VAR_SEQ 574 645 RAVLQAGCSRPWQEVLKDMVASDALDAQPLLDYFQPVTQWL
QEQNERNGEVLGWPEYQWRPPLPNNYPEGID -> MGQGWA
APGLPSLLLLLLCCGHSLLVPSRVAARRVTVNQGTTSQATT
TSKATTSIRATTHQTTAHQTTQSPN (in isoform
Testis-specific).
{ECO:0000303|PubMed:2550457}.
/FTId=VSP_037645.
MUTAGEN 727 727 K->E: No effect on activity. 20-fold
reduction in catalytic efficiency; when
associated with F-809.
{ECO:0000269|PubMed:7902354}.
MUTAGEN 809 809 Y->F: No effect on activity. 20-fold
reduction in catalytic efficiency; when
associated with E-727.
{ECO:0000269|PubMed:7902354}.
CONFLICT 48 48 E -> N (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 1310 AA; 150406 MW; 04777FAB17981DEA CRC64;
MGAAPGRRGP RLLRPPPPLL LLLLLLRPPP AALTLDPGLL PGDFAADEAG ARLFASSYNS
SAEQVLFRST AASWAHDTNI TAENARRQEE EALLSQEFAE AWGKKAKELY DPVWQNFTDP
ELRRIIGAVR TLGPANLPLA KRQQYNSLLS NMSQIYSTGK VCFPNKTASC WSLDPDLNNI
LASSRSYAML LFAWEGWHNA VGIPLKPLYQ EFTALSNEAY RQDGFSDTGA YWRSWYDSPT
FEEDLERIYH QLEPLYLNLH AYVRRVLHRR YGDRYINLRG PIPAHLLGNM WAQSWESIYD
MVVPFPDKPN LDVTSTMVQK GWNATHMFRV AEEFFTSLGL LPMPPEFWAE SMLEKPEDGR
EVVCHASAWD FYNRKDFRIK QCTQVTMDQL STVHHEMGHV QYYLQYKDQP VSLRRANPGF
HEAIGDVLAL SVSTPAHLHK IGLLDHVTND TESDINYLLK MALEKIAFLP FGYLVDQWRW
GVFSGRTPSS RYNFDWWYLR TKYQGICPPV VRNETHFDAG AKFHIPSVTP YIRYFVSFVL
QFQFHQALCM EAGHQGPLHQ CDIYQSTRAG AKLRAVLQAG CSRPWQEVLK DMVASDALDA
QPLLDYFQPV TQWLQEQNER NGEVLGWPEY QWRPPLPNNY PEGIDLVTDE AEASRFVEEY
DRSFQAVWNE YAEANWNYNT NITTEASKIL LQKNMQIANH TLTYGNWARR FDVSNFQNAT
SKRIIKKVQD LQRAVLPVKE LEEYNQILLD METIYSVANV CRVDGSCLQL EPDLTNLMAT
SRKYDELLWV WTSWRDKVGR AILPYFPKYV EFTNKAARLN GYVDAGDSWR SMYETPTLEQ
DLERLFQELQ PLYLNLHAYV GRALHRHYGA QHINLEGPIP AHLLGNMWAQ TWSNIYDLVA
PFPSASTMDA TEAMIKQGWT PRRMFEEADK FFISLGLLPV PPEFWNKSML EKPTDGREVV
CHASAWDFYN GKDFRIKQCT TVNMEDLVVV HHEMGHIQYF MQYKDLPVAL REGANPGFHE
AIGDVLALSV STPKHLHSIN LLSSEGGGYE HDINFLMKMA LDKIAFIPFS YLVDEWRWRV
FDGSITKENY NQEWWSLRLK YQGLCPPAPR SQGDFDPGAK FHIPSSVPYI RYFVSFIIQF
QFHEALCKAA GHTGPLHTCD IYQSKEAGKR LADAMKLGYS KPWPEAMKVI TGQPNMSASA
MMNYFKPLMD WLLTENGRHG EKLGWPQYTW TPNSARSEGS LPDSGRVNFL GMNLDAQQAR
VGQWVLLFLG VALLLASLGL TQRLFSIRYQ SLRQPHHGPQ FGSEVELRHS


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Pathways :
WP142: mRNA processing
WP1493: Carbon assimilation C4 pathway
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2344: vitamin B6 (pyridoxine, pyridoxal, pyridoxamine) biosynthesis and salvage pathway
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP376: Renin - Angiotensin System
WP626: Abscisic Acid Biosynthesis
WP1424: Globo Sphingolipid Metabolism
WP1857: Metabolism of water-soluble vitamins and cofactors
WP1963: The effect of Glucocorticoids on target gene expression
WP2328: Allograft rejection

Related Genes :
[ACE DCP DCP1] 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 Dcp1] 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 Dcp1] 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]
[Ance Race CG8827] Angiotensin-converting enzyme (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II)
[AGT SERPINA8] Angiotensinogen (Serpin A8) [Cleaved into: Angiotensin-1 (Angiotensin 1-10) (Angiotensin I) (Ang I); Angiotensin-2 (Angiotensin 1-8) (Angiotensin II) (Ang II); Angiotensin-3 (Angiotensin 2-8) (Angiotensin III) (Ang III) (Des-Asp[1]-angiotensin II); Angiotensin-4 (Angiotensin 3-8) (Angiotensin IV) (Ang IV); Angiotensin 1-9; Angiotensin 1-7; Angiotensin 1-5; Angiotensin 1-4]
[Acer CG10593] Angiotensin-converting enzyme-related protein (EC 3.4.15.1)
[Agt Serpina8] Angiotensinogen (Serpin A8) [Cleaved into: Angiotensin-1 (Angiotensin 1-10) (Angiotensin I) (Ang I); Angiotensin-2 (Angiotensin 1-8) (Angiotensin II) (Ang II); Angiotensin-3 (Angiotensin 2-8) (Angiotensin III) (Ang III) (Des-Asp[1]-angiotensin II); Angiotensin-4 (Angiotensin 3-8) (Angiotensin IV) (Ang IV); Angiotensin 1-9; Angiotensin 1-7; Angiotensin 1-5; Angiotensin 1-4]
[Agt Serpina8] Angiotensinogen (Serpin A8) [Cleaved into: Angiotensin-1 (Angiotensin 1-10) (Angiotensin I) (Ang I); Angiotensin-2 (Angiotensin 1-8) (Angiotensin II) (Ang II); Angiotensin-3 (Angiotensin 2-8) (Angiotensin III) (Ang III) (Des-Asp[1]-angiotensin II); Angiotensin-4 (Angiotensin 3-8) (Angiotensin IV) (Ang IV); Angiotensin 1-9; Angiotensin 1-7; Angiotensin 1-5; Angiotensin 1-4]
[] Bradykinin-potentiating and C-type natriuretic peptides (Angiotensin-converting enzyme inhibitor) (BPP-CNP homolog) [Cleaved into: Bradykinin-potentiating peptide 13a (BPP-13a) (Bradykinin-potentiating peptide S3,1); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Bradykinin-potentiating peptide S4,3,1); Bradykinin-potentiating peptide 12b (BPP-12b) (Bradykinin-potentiating peptide S4,3,2); Bradykinin-potentiating peptide 11e (BPP-11e); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide S5,2) (Bradykinin-potentiating peptide Va) (BPPVa) (Proline-rich peptide 5a) (PRO-5a); C-type natriuretic peptide (CNP)]
[] Bradykinin-potentiating and C-type natriuretic peptides (Angiotensin-converting enzyme inhibitor) (BPP-CNP homolog) [Cleaved into: Blomhotin; Bradykinin-potentiating peptide A (BPP-a) (Potentiator A); Leu3-blomhotin (Potentiator D); Bradykinin-potentiating peptide B (BPP-b) (Potentiator B); Bradykinin-potentiating peptide C (BPP-c) (Potentiator C); Bradykinin-potentiating peptide E (BPP-e) (Potentiator E); Bradykinin-potentiating peptide Ahb1 (BPP-Ahb1); Bradykinin-potentiating peptide Ahb2 (BPP-Ahb2); C-type natriuretic peptide]
[CORIN CRN TMPRSS10] Atrial natriuretic peptide-converting enzyme (EC 3.4.21.-) (Corin) (Heart-specific serine proteinase ATC2) (Pro-ANP-converting enzyme) (Transmembrane protease serine 10) [Cleaved into: Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Atrial natriuretic peptide-converting enzyme, activated protease fragment; Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment; Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment; Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment]
[Corin Crn Lrp4] Atrial natriuretic peptide-converting enzyme (EC 3.4.21.-) (Corin) (Low density lipoprotein receptor-related protein 4) (Pro-ANP-converting enzyme) [Cleaved into: Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Atrial natriuretic peptide-converting enzyme, activated protease fragment; Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[ACE] Angiotensin-converting enzyme (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[FAP] Prolyl endopeptidase FAP (EC 3.4.21.26) (170 kDa melanoma membrane-bound gelatinase) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]

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