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cGMP-inhibited 3',5'-cyclic phosphodiesterase B (EC 3.1.4.17) (CGIPDE1) (CGIP1) (Cyclic GMP-inhibited phosphodiesterase B) (CGI-PDE B)

 PDE3B_HUMAN             Reviewed;        1112 AA.
Q13370; B7ZM37; O00639; Q14408; Q6SEI4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
07-NOV-2018, entry version 175.
RecName: Full=cGMP-inhibited 3',5'-cyclic phosphodiesterase B;
EC=3.1.4.17;
AltName: Full=CGIPDE1;
Short=CGIP1;
AltName: Full=Cyclic GMP-inhibited phosphodiesterase B;
Short=CGI-PDE B;
Name=PDE3B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Adipose tissue;
PubMed=8884271; DOI=10.1006/geno.1996.0493;
Miki T., Taira M., Hockman S., Shimada F., Lieman J., Napolitano M.,
Ward D., Taira M., Makino H., Manganiello V.C.;
"Characterization of the cDNA and gene encoding human PDE3B, the cGIP1
isoform of the human cyclic GMP-inhibited cyclic nucleotide
phosphodiesterase family.";
Genomics 36:476-485(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8706823; DOI=10.1016/0014-5793(96)00410-3;
Murata T., Taira M., Manganiello V.C.;
"Differential expression of cGMP-inhibited cyclic nucleotide
phosphodiesterases in human hepatoma cell lines.";
FEBS Lett. 390:29-33(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-87.
PubMed=8921398; DOI=10.1006/geno.1996.0544;
Loebbert R.W., Winterpacht A., Seipel B., Zabel B.U.;
"Molecular cloning and chromosomal assignment of the human homologue
of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A) -- a gene
involved in fat metabolism located at 11p15.1.";
Genomics 37:211-218(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=16702214; DOI=10.1074/jbc.M601307200;
Liu H., Tang J.R., Choi Y.H., Napolitano M., Hockman S., Taira M.,
Degerman E., Manganiello V.C.;
"Importance of cAMP-response element-binding protein in regulation of
expression of the murine cyclic nucleotide phosphodiesterase 3B
(Pde3b) gene in differentiating 3T3-L1 preadipocytes.";
J. Biol. Chem. 281:21096-21113(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
FUNCTION, INTERACTION WITH RAPGEF3 AND PIK3R6, AND MUTAGENESIS OF
ARG-2; ARG-3; ARG-6; ALA-8; LYS-9; ALA-10; ARG-12; ARG-439; ARG-440;
SER-445 AND PRO-449.
PubMed=21393242; DOI=10.1074/jbc.M110.217026;
Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A.,
Zaccolo M., Houslay M.D., Maurice D.H.;
"A phosphodiesterase 3B-based signaling complex integrates exchange
protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals
in human arterial endothelial cells.";
J. Biol. Chem. 286:16285-16296(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 654-1073 IN COMPLEX WITH
METAL IONS AND INHIBITORS, FUNCTION, AND COFACTOR.
PubMed=15147193; DOI=10.1021/bi049868i;
Scapin G., Patel S.B., Chung C., Varnerin J.P., Edmondson S.D.,
Mastracchio A., Parmee E.R., Singh S.B., Becker J.W.,
Van der Ploeg L.H., Tota M.R.;
"Crystal structure of human phosphodiesterase 3B: atomic basis for
substrate and inhibitor specificity.";
Biochemistry 43:6091-6100(2004).
-!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
specificity for the second messengers cAMP and cGMP, which are key
regulators of many important physiological processes. May play a
role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through
simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling
complex in which the PI3K gamma complex is activated by RAPGEF3
and which is involved in angiogenesis.
{ECO:0000269|PubMed:15147193, ECO:0000269|PubMed:21393242}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000269|PubMed:15147193};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000269|PubMed:15147193};
-!- ACTIVITY REGULATION: Inhibited by cGMP.
-!- SUBUNIT: Interacts with PIK3CG (By similarity). Interacts with
RAPGEF3 and PIK3R6. {ECO:0000250, ECO:0000269|PubMed:15147193,
ECO:0000269|PubMed:21393242}.
-!- INTERACTION:
P48736:PIK3CG; NbExp=3; IntAct=EBI-6172856, EBI-1030384;
Q5UE93:PIK3R6; NbExp=3; IntAct=EBI-6172856, EBI-6172907;
O95398:RAPGEF3; NbExp=8; IntAct=EBI-6172856, EBI-6172806;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13370-1; Sequence=Displayed;
Name=2;
IsoId=Q13370-2; Sequence=VSP_054138;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Abundant in adipose tissues.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE3 subfamily. {ECO:0000305}.
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EMBL; U38178; AAC50724.1; -; Genomic_DNA.
EMBL; D50640; BAA09306.1; -; Genomic_DNA.
EMBL; X95520; CAA64774.1; -; mRNA.
EMBL; AY459346; AAR24292.1; -; mRNA.
EMBL; AC018795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68474.1; -; Genomic_DNA.
EMBL; BC136565; AAI36566.1; -; mRNA.
EMBL; BC136566; AAI36567.1; -; mRNA.
EMBL; BC144248; AAI44249.1; -; mRNA.
CCDS; CCDS7817.1; -. [Q13370-1]
PIR; S70522; S70522.
RefSeq; NP_000913.2; NM_000922.3. [Q13370-1]
UniGene; Hs.445711; -.
PDB; 1SO2; X-ray; 2.40 A; A/B/C/D=654-1073.
PDB; 1SOJ; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=654-1073.
PDBsum; 1SO2; -.
PDBsum; 1SOJ; -.
ProteinModelPortal; Q13370; -.
SMR; Q13370; -.
BioGrid; 111166; 46.
IntAct; Q13370; 6.
STRING; 9606.ENSP00000282096; -.
BindingDB; Q13370; -.
ChEMBL; CHEMBL290; -.
DrugBank; DB07954; 3-isobutyl-1-methyl-7H-xanthine.
DrugBank; DB00201; Caffeine.
GuidetoPHARMACOLOGY; 1299; -.
iPTMnet; Q13370; -.
PhosphoSitePlus; Q13370; -.
BioMuta; PDE3B; -.
DMDM; 143811435; -.
EPD; Q13370; -.
MaxQB; Q13370; -.
PaxDb; Q13370; -.
PeptideAtlas; Q13370; -.
PRIDE; Q13370; -.
ProteomicsDB; 59354; -.
Ensembl; ENST00000282096; ENSP00000282096; ENSG00000152270. [Q13370-1]
Ensembl; ENST00000455098; ENSP00000388644; ENSG00000152270. [Q13370-2]
GeneID; 5140; -.
KEGG; hsa:5140; -.
UCSC; uc001mln.4; human. [Q13370-1]
CTD; 5140; -.
DisGeNET; 5140; -.
EuPathDB; HostDB:ENSG00000152270.8; -.
GeneCards; PDE3B; -.
HGNC; HGNC:8779; PDE3B.
HPA; HPA056111; -.
MIM; 602047; gene.
neXtProt; NX_Q13370; -.
OpenTargets; ENSG00000152270; -.
PharmGKB; PA33127; -.
eggNOG; ENOG410IEGG; Eukaryota.
eggNOG; ENOG410XT2V; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000060144; -.
HOVERGEN; HBG053541; -.
KO; K13296; -.
OMA; CAFFFLT; -.
OrthoDB; EOG091G0BTI; -.
PhylomeDB; Q13370; -.
TreeFam; TF329631; -.
BRENDA; 3.1.4.17; 2681.
Reactome; R-HSA-165160; PDE3B signalling.
Reactome; R-HSA-418457; cGMP effects.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SignaLink; Q13370; -.
SIGNOR; Q13370; -.
ChiTaRS; PDE3B; human.
EvolutionaryTrace; Q13370; -.
GenomeRNAi; 5140; -.
PRO; PR:Q13370; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000152270; Expressed in 165 organ(s), highest expression level in adipose tissue.
CleanEx; HS_PDE3B; -.
Genevisible; Q13370; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; EXP:Reactome.
GO; GO:0004119; F:cGMP-inhibited cyclic-nucleotide phosphodiesterase activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043422; F:protein kinase B binding; ISS:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; TAS:BHF-UCL.
GO; GO:0007162; P:negative regulation of cell adhesion; IMP:BHF-UCL.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IC:BHF-UCL.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:BHF-UCL.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; cAMP; cGMP;
Complete proteome; Hydrolase; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 1112 cGMP-inhibited 3',5'-cyclic
phosphodiesterase B.
/FTId=PRO_0000198802.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255}.
TRANSMEM 192 212 Helical. {ECO:0000255}.
TRANSMEM 220 240 Helical. {ECO:0000255}.
TRANSMEM 247 267 Helical. {ECO:0000255}.
DOMAIN 651 1079 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
REGION 1 25 Interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
REGION 436 460 Interaction with PIK3R6.
{ECO:0000269|PubMed:21393242}.
COMPBIAS 1077 1080 Poly-Glu.
ACT_SITE 737 737 Proton donor. {ECO:0000250}.
METAL 741 741 Divalent metal cation 1.
METAL 821 821 Divalent metal cation 1.
METAL 822 822 Divalent metal cation 1.
METAL 822 822 Divalent metal cation 2.
METAL 937 937 Divalent metal cation 1.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q61409}.
MOD_RES 295 295 Phosphoserine; by PKB/AKT1 or PKB/AKT2.
{ECO:0000250|UniProtKB:Q61409}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:Q61409}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 376 426 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054138.
VARIANT 87 87 A -> V (in dbSNP:rs1056584).
{ECO:0000269|PubMed:8921398}.
/FTId=VAR_031462.
MUTAGEN 2 2 R->A: Abolishes interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 3 3 R->A: Abolishes interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 6 6 R->A: Abolishes interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 8 8 A->D: Impairs interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 9 9 K->A: Abolishes interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 10 10 A->D: Impairss interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 12 12 R->A: Abolishes interaction with RAPGEF3.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 439 439 R->A: Impairss interaction with PIK3R6.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 440 440 R->A: Impairss interaction with PIK3R6.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 445 445 S->A: Impairss interaction with PIK3R6.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 449 449 P->A: Impairss interaction with PIK3R6.
{ECO:0000269|PubMed:21393242}.
CONFLICT 84 84 A -> D (in Ref. 1; AAC50724 and 2;
BAA09306). {ECO:0000305}.
HELIX 662 674 {ECO:0000244|PDB:1SO2}.
HELIX 681 688 {ECO:0000244|PDB:1SO2}.
HELIX 689 694 {ECO:0000244|PDB:1SO2}.
HELIX 695 706 {ECO:0000244|PDB:1SO2}.
HELIX 709 712 {ECO:0000244|PDB:1SO2}.
HELIX 717 728 {ECO:0000244|PDB:1SO2}.
STRAND 735 738 {ECO:0000244|PDB:1SO2}.
HELIX 739 752 {ECO:0000244|PDB:1SO2}.
HELIX 802 804 {ECO:0000244|PDB:1SO2}.
HELIX 808 820 {ECO:0000244|PDB:1SO2}.
TURN 821 824 {ECO:0000244|PDB:1SO2}.
HELIX 830 835 {ECO:0000244|PDB:1SO2}.
HELIX 839 843 {ECO:0000244|PDB:1SO2}.
TURN 844 846 {ECO:0000244|PDB:1SO2}.
HELIX 849 863 {ECO:0000244|PDB:1SO2}.
HELIX 866 868 {ECO:0000244|PDB:1SO2}.
TURN 870 873 {ECO:0000244|PDB:1SO2}.
HELIX 876 891 {ECO:0000244|PDB:1SO2}.
HELIX 895 897 {ECO:0000244|PDB:1SO2}.
HELIX 898 909 {ECO:0000244|PDB:1SO2}.
STRAND 911 913 {ECO:0000244|PDB:1SO2}.
HELIX 922 937 {ECO:0000244|PDB:1SO2}.
HELIX 940 942 {ECO:0000244|PDB:1SO2}.
HELIX 945 968 {ECO:0000244|PDB:1SO2}.
HELIX 984 994 {ECO:0000244|PDB:1SO2}.
HELIX 996 1005 {ECO:0000244|PDB:1SO2}.
STRAND 1012 1015 {ECO:0000244|PDB:1SOJ}.
STRAND 1055 1058 {ECO:0000244|PDB:1SO2}.
HELIX 1060 1072 {ECO:0000244|PDB:1SO2}.
SEQUENCE 1112 AA; 124333 MW; 55451C3DA142EF6A CRC64;
MRRDERDAKA MRSLQPPDGA GSPPESLRNG YVKSCVSPLR QDPPRGFFFH LCRFCNVELR
PPPASPQQPR RCSPFCRARL SLGALAAFVL ALLLGAEPES WAAGAAWLRT LLSVCSHSLS
PLFSIACAFF FLTCFLTRTK RGPGPGRSCG SWWLLALPAC CYLGDFLVWQ WWSWPWGDGD
AGSAAPHTPP EAAAGRLLLV LSCVGLLLTL AHPLRLRHCV LVLLLASFVW WVSFTSLGSL
PSALRPLLSG LVGGAGCLLA LGLDHFFQIR EAPLHPRLSS AAEEKVPVIR PRRRSSCVSL
GETAASYYGS CKIFRRPSLP CISREQMILW DWDLKQWYKP HYQNSGGGNG VDLSVLNEAR
NMVSDLLTDP SLPPQVISSL RSISSLMGAF SGSCRPKINP LTPFPGFYPC SEIEDPAEKG
DRKLNKGLNR NSLPTPQLRR SSGTSGLLPV EQSSRWDRNN GKRPHQEFGI SSQGCYLNGP
FNSNLLTIPK QRSSSVSLTH HVGLRRAGVL SSLSPVNSSN HGPVSTGSLT NRSPIEFPDT
ADFLNKPSVI LQRSLGNAPN TPDFYQQLRN SDSNLCNSCG HQMLKYVSTS ESDGTDCCSG
KSGEEENIFS KESFKLMETQ QEEETEKKDS RKLFQEGDKW LTEEAQSEQQ TNIEQEVSLD
LILVEEYDSL IEKMSNWNFP IFELVEKMGE KSGRILSQVM YTLFQDTGLL EIFKIPTQQF
MNYFRALENG YRDIPYHNRI HATDVLHAVW YLTTRPVPGL QQIHNGCGTG NETDSDGRIN
HGRIAYISSK SCSNPDESYG CLSSNIPALE LMALYVAAAM HDYDHPGRTN AFLVATNAPQ
AVLYNDRSVL ENHHAASAWN LYLSRPEYNF LLHLDHVEFK RFRFLVIEAI LATDLKKHFD
FLAEFNAKAN DVNSNGIEWS NENDRLLVCQ VCIKLADING PAKVRDLHLK WTEGIVNEFY
EQGDEEANLG LPISPFMDRS SPQLAKLQES FITHIVGPLC NSYDAAGLLP GQWLEAEEDN
DTESGDDEDG EELDTEDEEM ENNLNPKPPR RKSRRRIFCQ LMHHLTENHK IWKEIVEEEE
KCKADGNKLQ VENSSLPQAD EIQVIEEADE EE


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E1933h Rat ELISA Kit FOR cGMP-inhibited 3',5'-cyclic phosphodiesterase B 96T
PDE3B_HUMAN Human ELISA Kit FOR cGMP-inhibited 3',5'-cyclic phosphodiesterase B 96T
PDE3A_HUMAN ELISA Kit FOR cGMP-inhibited 3',5'-cyclic phosphodiesterase A; organism: Human; gene name: PDE3A 96T
PDE3B_HUMAN ELISA Kit FOR cGMP-inhibited 3',5'-cyclic phosphodiesterase B; organism: Human; gene name: PDE3B 96T
PDE3B_MOUSE ELISA Kit FOR cGMP-inhibited 3',5'-cyclic phosphodiesterase B; organism: Mouse; gene name: Pde3b 96T
PDE3A_MOUSE ELISA Kit FOR cGMP-inhibited 3',5'-cyclic phosphodiesterase A; organism: Mouse; gene name: Pde3a 96T
18-783-75548 RABBIT ANTI HUMAN PHOSPHODIESTERASE 3A - PDE3A; EC 3.1.4.17; Cyclic GMP-inhibited phosphodiesterase A; CGI-PDE A Polyclonal 0.05 mg
EH1324 cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A Elisa Kit 96T
CSB-EL017681HU Human cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A) ELISA kit 96T
EIAAB30284 cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A,Mouse,Mus musculus,Pde10a
EIAAB30283 cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A,Pde10a,Rat,Rattus norvegicus
EIAAB30285 cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A,Homo sapiens,Human,PDE10A
E1158m ELISA Kit FOR cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A; organism: Mouse; gene name: Pde10a 96T
E1158h ELISA Kit FOR cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A; organism: Human; gene name: PDE10A 96T
EIAAB30305 cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,Homo sapiens,Human,PDE2A
EIAAB30306 Bos taurus,Bovine,cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,PDE2A
EIAAB30303 cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,Pde2a,Rat,Rattus norvegicus
EIAAB30304 cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,Mouse,Mus musculus,Pde2a
EIAAB30339 cGMP phosphodiesterase 6C,Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha',Mouse,Mus musculus,Pde6c


 

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