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Adenylate cyclase type 3 (EC 4.6.1.1) (ATP pyrophosphate-lyase 3) (Adenylate cyclase type III) (AC-III) (Adenylate cyclase, olfactive type) (Adenylyl cyclase 3) (AC3)

 ADCY3_HUMAN             Reviewed;        1144 AA.
O60266; B3KT86; Q53T54; Q9UDB1;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 3.
18-JUL-2018, entry version 181.
RecName: Full=Adenylate cyclase type 3;
EC=4.6.1.1;
AltName: Full=ATP pyrophosphate-lyase 3;
AltName: Full=Adenylate cyclase type III;
Short=AC-III;
AltName: Full=Adenylate cyclase, olfactive type;
AltName: Full=Adenylyl cyclase 3 {ECO:0000305};
Short=AC3 {ECO:0000303|PubMed:9920776};
Name=ADCY3; Synonyms=KIAA0511;
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), VARIANT PRO-107, AND TISSUE
SPECIFICITY.
TISSUE=Fetal brain;
PubMed=9920776; DOI=10.1006/bbrc.1998.9983;
Yang B., He B., Abdel-Halim S.M., Tibell A., Brendel M.D.,
Bretzel R.G., Efendic S., Hillert J.;
"Molecular cloning of a full-length cDNA for human type 3 adenylyl
cyclase and its expression in human islets.";
Biochem. Biophys. Res. Commun. 254:548-551(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Substantia nigra;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-1144 (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 984-1060 (ISOFORM 1/2).
PubMed=8476432; DOI=10.1006/bbrc.1993.1415;
Hellevuo K., Yoshimura M., Kao M., Hoffman P.L., Cooper D.M.F.,
Tabakoff B.;
"A novel adenylyl cyclase sequence cloned from the human
erythroleukemia cell line.";
Biochem. Biophys. Res. Commun. 192:311-318(1993).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11549699; DOI=10.1210/jcem.86.9.7837;
Cote M., Guillon G., Payet M.D., Gallo-Payet N.;
"Expression and regulation of adenylyl cyclase isoforms in the human
adrenal gland.";
J. Clin. Endocrinol. Metab. 86:4495-4503(2001).
[8]
TISSUE SPECIFICITY.
PubMed=15705663; DOI=10.1210/me.2004-0318;
Livera G., Xie F., Garcia M.A., Jaiswal B., Chen J., Law E.,
Storm D.R., Conti M.;
"Inactivation of the mouse adenylyl cyclase 3 gene disrupts male
fertility and spermatozoon function.";
Mol. Endocrinol. 19:1277-1290(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
in response to G-protein signaling. Participates in signaling
cascades triggered by odorant receptors via its function in cAMP
biosynthesis. Required for the perception of odorants. Required
for normal sperm motility and normal male fertility. Plays a role
in regulating insulin levels and body fat accumulation in response
to a high fat diet. {ECO:0000250|UniProtKB:Q8VHH7}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P30803};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:P30803};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ENZYME REGULATION: Activated by forskolin. After forskolin
treatment, activity is further increased by calcium/calmodulin. In
the absence of forskolin, calcium/calmodulin has little effect on
enzyme activity. {ECO:0000250|UniProtKB:P21932}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11549699};
Multi-pass membrane protein {ECO:0000305}. Cytoplasm
{ECO:0000269|PubMed:11549699}. Cell projection, cilium
{ECO:0000250|UniProtKB:Q8VHH7}. Golgi apparatus
{ECO:0000250|UniProtKB:P21932}. Note=Also detected in the
cytoplasm, close to lipid droplets. {ECO:0000269|PubMed:11549699}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60266-1; Sequence=Displayed;
Name=2;
IsoId=O60266-2; Sequence=VSP_055813, VSP_055814, VSP_055815;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in zona glomerulosa and zona
fasciculata in the adrenal gland (at protein level)
(PubMed:11549699). Expressed in brain, heart, kidney, liver, lung,
pancreas islets, placenta, and skeletal muscle (PubMed:9920776).
Detected in testis (PubMed:15705663).
{ECO:0000269|PubMed:11549699, ECO:0000269|PubMed:15705663,
ECO:0000269|PubMed:9920776}.
-!- DOMAIN: The protein contains two modules with six transmembrane
helices each; both are required for catalytic activity. Isolated
N-terminal or C-terminal modules have no catalytic activity, but
when they are brought together, enzyme activity is restored. The
active site is at the interface of the two modules.
{ECO:0000250|UniProtKB:P30803}.
-!- PTM: Sumoylated. Sumoylation is required for targeting ot
olfactory cilia. {ECO:0000250|UniProtKB:P21932}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8VHH7}.
-!- PTM: Rapidly phosphorylated after stimulation by odorants or
forskolin. Phosphorylation by CaMK2 at Ser-1076 down-regulates
enzyme activity. {ECO:0000250|UniProtKB:Q8VHH7}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; AF033861; AAD13403.1; -; mRNA.
EMBL; AK095173; BAG52998.1; -; mRNA.
EMBL; AC012073; AAY14787.1; -; Genomic_DNA.
EMBL; BC126235; AAI26236.1; -; mRNA.
EMBL; AB011083; BAA25437.1; -; mRNA.
CCDS; CCDS1715.1; -. [O60266-1]
RefSeq; NP_001307542.1; NM_001320613.1.
RefSeq; NP_004027.2; NM_004036.4. [O60266-1]
UniGene; Hs.467898; -.
UniGene; Hs.611397; -.
ProteinModelPortal; O60266; -.
SMR; O60266; -.
BioGrid; 106623; 17.
IntAct; O60266; 2.
MINT; O60266; -.
STRING; 9606.ENSP00000260600; -.
ChEMBL; CHEMBL2097167; -.
iPTMnet; O60266; -.
PhosphoSitePlus; O60266; -.
BioMuta; ADCY3; -.
EPD; O60266; -.
MaxQB; O60266; -.
PaxDb; O60266; -.
PeptideAtlas; O60266; -.
PRIDE; O60266; -.
ProteomicsDB; 49298; -.
DNASU; 109; -.
Ensembl; ENST00000260600; ENSP00000260600; ENSG00000138031. [O60266-1]
GeneID; 109; -.
KEGG; hsa:109; -.
UCSC; uc002rfs.5; human. [O60266-1]
CTD; 109; -.
DisGeNET; 109; -.
EuPathDB; HostDB:ENSG00000138031.14; -.
GeneCards; ADCY3; -.
H-InvDB; HIX0001880; -.
H-InvDB; HIX0030389; -.
H-InvDB; HIX0161886; -.
HGNC; HGNC:234; ADCY3.
HPA; CAB010223; -.
MIM; 600291; gene.
neXtProt; NX_O60266; -.
OpenTargets; ENSG00000138031; -.
PharmGKB; PA164741137; -.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
GeneTree; ENSGT00760000119042; -.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; O60266; -.
KO; K08043; -.
PhylomeDB; O60266; -.
TreeFam; TF313845; -.
Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
Reactome; R-HSA-163615; PKA activation.
Reactome; R-HSA-164378; PKA activation in glucagon signalling.
Reactome; R-HSA-170660; Adenylate cyclase activating pathway.
Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-442720; CREB phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
SIGNOR; O60266; -.
GeneWiki; ADCY3; -.
GenomeRNAi; 109; -.
PRO; PR:O60266; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138031; -.
CleanEx; HS_ADCY3; -.
ExpressionAtlas; O60266; baseline and differential.
Genevisible; O60266; HS.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007340; P:acrosome reaction; ISS:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0008355; P:olfactory learning; ISS:UniProtKB.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0007608; P:sensory perception of smell; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
Gene3D; 3.30.70.1230; -; 2.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR032628; AC_N.
InterPro; IPR030672; Adcy.
InterPro; IPR029787; Nucleotide_cyclase.
Pfam; PF16214; AC_N; 1.
Pfam; PF00211; Guanylate_cyc; 2.
PIRSF; PIRSF039050; Ade_cyc; 1.
SMART; SM00044; CYCc; 2.
SUPFAM; SSF55073; SSF55073; 2.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calmodulin-binding;
cAMP biosynthesis; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Glycoprotein; Golgi apparatus; Isopeptide bond; Lyase;
Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
Olfaction; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Sensory transduction; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 1144 Adenylate cyclase type 3.
/FTId=PRO_0000195687.
TOPO_DOM 1 79 Cytoplasmic. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TRANSMEM 173 193 Helical. {ECO:0000255}.
TRANSMEM 226 246 Helical. {ECO:0000255}.
TRANSMEM 381 401 Helical. {ECO:0000255}.
TOPO_DOM 402 632 Cytoplasmic. {ECO:0000255}.
TRANSMEM 633 653 Helical. {ECO:0000255}.
TRANSMEM 664 684 Helical. {ECO:0000255}.
TRANSMEM 708 728 Helical. {ECO:0000255}.
TRANSMEM 754 774 Helical. {ECO:0000255}.
TRANSMEM 775 795 Helical. {ECO:0000255}.
TRANSMEM 833 853 Helical. {ECO:0000255}.
TOPO_DOM 854 1144 Cytoplasmic. {ECO:0000255}.
NP_BIND 324 329 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 366 368 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1062 1064 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1069 1073 ATP. {ECO:0000250|UniProtKB:P26769}.
METAL 324 324 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 324 324 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 325 325 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 368 368 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 368 368 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 412 412 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 975 975 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1109 1109 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VHH7}.
MOD_RES 1076 1076 Phosphoserine; by CaMK2.
{ECO:0000250|UniProtKB:Q8VHH7}.
CARBOHYD 736 736 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 465 465 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3).
{ECO:0000250|UniProtKB:P21932}.
VAR_SEQ 1 389 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055813.
VAR_SEQ 452 452 G -> GGSKIEERLYSCVVAPTLRLRWE (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_055814.
VAR_SEQ 725 770 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055815.
VARIANT 107 107 S -> P (in dbSNP:rs11676272).
{ECO:0000269|PubMed:9920776}.
/FTId=VAR_048248.
SEQUENCE 1144 AA; 128960 MW; B75D39DD0A8ACA12 CRC64;
MPRNQGFSEP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP RFMRLTFVPE
SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF SSDKLASLAV AGIGLVLDII
LFVLCKKGLL PDRVTRRVLP YVLWLLITAQ IFSYLGLNFA RAHAASDTVG WQVFFVFSFF
ITLPLSLSPI VIISVVSCVV HTLVLGVTVA QQQQEELKGM QLLREILANV FLYLCAIAVG
IMSYYMADRK HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR FDKLAAKYHQ
LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY VREKTKTGVD MRVGVHTGTV
LGGVLGQKRW QYDVWSTDVT VANKMEAGGI PGRVHISQST MDCLKGEFDV EPGDGGSRCD
YLEEKGIETY LIIASKPEVK KTATQNGLNG SALPNGAPAS SKSSSPALIE TKEPNGSAHS
SGSTSEKPEE QDAQADNPSF PNPRRRLRLQ DLADRVVDAS EDEHELNQLL NEALLERESA
QVVKKRNTFL LSMRFMDPEM ETRYSVEKEK QSGAAFSCSC VVLLCTALVE ILIDPWLMTN
YVTFMVGEIL LLILTICSLA AIFPRAFPKK LVAFSTWIDR TRWARNTWAM LAIFILVMAN
VVDMLSCLQY YTGPSNATAG METEGSCLEN PKYYNYVAVL SLIATIMLVQ VSHMVKLTLM
LLVAGAVATI NLYAWRPVFD EYDHKRFREH DLPMVALEQM QGFNPGLNGT DRLPLVPSKY
SMTVMVFLMM LSFYYFSRHV EKLARTLFLW KIEVHDQKER VYEMRRWNEA LVTNMLPEHV
ARHFLGSKKR DEELYSQTYD EIGVMFASLP NFADFYTEES INNGGIECLR FLNEIISDFD
SLLDNPKFRV ITKIKTIGST YMAASGVTPD VNTNGFASSN KEDKSERERW QHLADLADFA
LAMKDTLTNI NNQSFNNFML RIGMNKGGVL AGVIGARKPH YDIWGNTVNV ASRMESTGVM
GNIQVVEETQ VILREYGFRF VRRGPIFVKG KGELLTFFLK GRDKLATFPN GPSVTLPHQV
VDNS


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E1349h ELISA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
E1349h ELISA kit ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
U1349h CLIA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Homo sapiens,Human 96T
U1349b CLIA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Bos taurus,Bovine,Ca(2+)_calmodulin-activated adenylyl cyclase 96T
E1349m ELISA Adcy1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Mouse,Mus musculus 96T
E1349m ELISA kit Adcy1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Mouse,Mus musculus 96T
E1349b ELISA ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Bos taurus,Bovine,Ca(2+)_calmodulin-activated adenylyl cyclase 96T
U1349m CLIA Adcy1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Ca(2+)_calmodulin-activated adenylyl cyclase,Mouse,Mus musculus 96T
E1349b ELISA kit ADCY1,Adenylate cyclase type 1,Adenylate cyclase type I,Adenylyl cyclase 1,ATP pyrophosphate-lyase 1,Bos taurus,Bovine,Ca(2+)_calmodulin-activated adenylyl cyclase 96T
15-288-21024 Adenylate cyclase type 6 - EC 4.6.1.1; Adenylate cyclase type VI; ATP pyrophosphate-lyase 6; Ca(2+)-inhibitable adenylyl cyclase Polyclonal 0.05 mg
15-288-21024 Adenylate cyclase type 6 - EC 4.6.1.1; Adenylate cyclase type VI; ATP pyrophosphate-lyase 6; Ca(2+)-inhibitable adenylyl cyclase Polyclonal 0.1 mg
U1348h CLIA ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348h ELISA ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348h ELISA kit ADCY10,Adenylate cyclase homolog,Adenylate cyclase type 10,AH-related protein,Germ cell soluble adenylyl cyclase,Homo sapiens,hsAC,Human,sAC,SAC,Testicular soluble adenylyl cyclase 96T
U1348Rb CLIA ADCY10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Oryctolagus cuniculus,Rabbit,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348m ELISA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Mouse,Mus musculus,sAC,Sac,Sacy,Testicular soluble adenylyl cyclase 96T
E1348Rb ELISA ADCY10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Oryctolagus cuniculus,Rabbit,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348Rb ELISA kit ADCY10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Oryctolagus cuniculus,Rabbit,sAC,SAC,Testicular soluble adenylyl cyclase 96T
E1348m ELISA kit Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Mouse,Mus musculus,sAC,Sac,Sacy,Testicular soluble adenylyl cyclase 96T
U1348m CLIA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Mouse,Mus musculus,sAC,Sac,Sacy,Testicular soluble adenylyl cyclase 96T
U1348r CLIA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Rat,Rattus norvegicus,sAC,Sac,Testicular soluble adenylyl cyclase 96T
E1348r ELISA Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Rat,Rattus norvegicus,sAC,Sac,Testicular soluble adenylyl cyclase 96T
E1348r ELISA kit Adcy10,Adenylate cyclase type 10,Germ cell soluble adenylyl cyclase,Rat,Rattus norvegicus,sAC,Sac,Testicular soluble adenylyl cyclase 96T
136134-68-4 adenylate cyclase activating peptide frag adenylate cyclase activ 1g
127317-03-7 adenylate cyclase activating peptide_27 adenylate cyclase activ 1g


 

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