Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

cAMP-specific 3',5'-cyclic phosphodiesterase 4D (EC 3.1.4.53) (DPDE3)

 PDE4D_MOUSE             Reviewed;         747 AA.
Q01063; B2KF58; Q6TRH9; Q8C4Q7; Q8CG05;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
23-MAY-2018, entry version 158.
RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4D;
EC=3.1.4.53;
AltName: Full=DPDE3;
Name=Pde4d;
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 7), AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=12834813; DOI=10.1016/S0898-6568(03)00042-1;
Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C.,
Xin X., Hu Y., Unterbeck A., De Vivo M.;
"Cloning and characterization of novel PDE4D isoforms PDE4D6 and
PDE4D7.";
Cell. Signal. 15:883-891(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
Chai H., Gaweda B., De Vivo M., Wang D.;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 400-514.
PubMed=1326532;
Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
"A polymerase chain reaction strategy to identify and clone cyclic
nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA
encoding the 63-kDa calmodulin-dependent phosphodiesterase.";
J. Biol. Chem. 267:18683-18688(1992).
[6]
INTERACTION WITH SHANK2, AND TISSUE SPECIFICITY.
PubMed=17244609; DOI=10.1074/jbc.M610857200;
Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M.,
Lee M.G.;
"Dynamic regulation of cystic fibrosis transmembrane conductance
regulator by competitive interactions of molecular adaptors.";
J. Biol. Chem. 282:10414-10422(2007).
[7]
IDENTIFICATION IN A COMPLEX WITH RYR1; FKBP1A; PKA AND PP1.
PubMed=18268335; DOI=10.1073/pnas.0711074105;
Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X.,
Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A.,
Marks A.R.;
"Remodeling of ryanodine receptor complex causes 'leaky' channels: a
molecular mechanism for decreased exercise capacity.";
Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
Spleen;
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).
-!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
regulator of many important physiological processes.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
adenosine 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
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:0000250};
-!- ENZYME REGULATION: Inhibited by rolipram. Activated by
phosphatidic acid (By similarity). {ECO:0000250}.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- SUBUNIT: Homodimer for the long isoforms. Isoforms with truncated
N-termini are monomeric. Binds ARRB2. Interacts with PDE4DIP (By
similarity). Identified in a complex composed of RYR1, PDE4D, PKA,
FKBP1A and protein phosphatase 1 (PP1). Interacts (via N-terminal
region) with SHANK2 (via proline-rich region); the interaction is
increased in a PKA-dependent manner. {ECO:0000250,
ECO:0000269|PubMed:17244609, ECO:0000269|PubMed:18268335}.
-!- INTERACTION:
P34971:Adrb1; NbExp=3; IntAct=EBI-7764239, EBI-7764182;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Cytoplasm,
cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome. Apical cell membrane {ECO:0000250}.
Note=Colocalized with SHANK2 to the apical membrane of colonic
crypt cells (By similarity). Found in the soluble fraction,
associated with membranes, and associated with the cytoskeleton
and the centrosome. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=7; Synonyms=PDE4D7;
IsoId=Q01063-1; Sequence=Displayed;
Name=9; Synonyms=PDE4D9;
IsoId=Q01063-2; Sequence=VSP_012395, VSP_012396;
Name=3;
IsoId=Q01063-3; Sequence=VSP_012394, VSP_012397;
-!- TISSUE SPECIFICITY: Expressed in brain (at protein level). Isoform
7 is detected in heart, brain, lung, kidney and testis.
{ECO:0000269|PubMed:12834813, ECO:0000269|PubMed:17244609}.
-!- INDUCTION: Up-regulated by cAMP and follicle-stimulating hormone.
{ECO:0000250}.
-!- PTM: Sumoylation of long isoforms by PIAS4 augments their
activation by PKA phosphorylation and represses their inhibition
by ERK phosphorylation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF536978; AAN10120.1; -; mRNA.
EMBL; AY388962; AAQ90406.1; -; mRNA.
EMBL; AK081466; BAC38226.1; -; mRNA.
EMBL; CT025605; CAQ51656.1; -; Genomic_DNA.
EMBL; AC161585; CAQ51656.1; JOINED; Genomic_DNA.
EMBL; AC163650; CAQ51656.1; JOINED; Genomic_DNA.
EMBL; M94541; AAA37368.1; ALT_TERM; mRNA.
CCDS; CCDS49359.1; -. [Q01063-1]
RefSeq; NP_035186.1; NM_011056.3. [Q01063-1]
RefSeq; XP_006517710.1; XM_006517647.2. [Q01063-2]
UniGene; Mm.434429; -.
ProteinModelPortal; Q01063; -.
SMR; Q01063; -.
BioGrid; 232023; 3.
DIP; DIP-29706N; -.
IntAct; Q01063; 6.
MINT; Q01063; -.
STRING; 10090.ENSMUSP00000113488; -.
ChEMBL; CHEMBL2111373; -.
iPTMnet; Q01063; -.
PhosphoSitePlus; Q01063; -.
MaxQB; Q01063; -.
PaxDb; Q01063; -.
PRIDE; Q01063; -.
Ensembl; ENSMUST00000074103; ENSMUSP00000073742; ENSMUSG00000021699. [Q01063-2]
Ensembl; ENSMUST00000120664; ENSMUSP00000113024; ENSMUSG00000021699. [Q01063-3]
Ensembl; ENSMUST00000122041; ENSMUSP00000113488; ENSMUSG00000021699. [Q01063-1]
Ensembl; ENSMUST00000177907; ENSMUSP00000136485; ENSMUSG00000021699. [Q01063-1]
GeneID; 238871; -.
KEGG; mmu:238871; -.
UCSC; uc007rvg.2; mouse. [Q01063-1]
UCSC; uc007rvj.2; mouse. [Q01063-2]
CTD; 5144; -.
MGI; MGI:99555; Pde4d.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000118889; -.
HOGENOM; HOG000236297; -.
HOVERGEN; HBG108239; -.
InParanoid; Q01063; -.
KO; K13293; -.
OMA; QHEVEMP; -.
PhylomeDB; Q01063; -.
BRENDA; 3.1.4.53; 3474.
Reactome; R-MMU-180024; DARPP-32 events.
Reactome; R-MMU-418555; G alpha (s) signalling events.
UniPathway; UPA00762; UER00747.
ChiTaRS; Pde4d; mouse.
PRO; PR:Q01063; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021699; -.
CleanEx; MM_PDE4D; -.
ExpressionAtlas; Q01063; baseline and differential.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:BHF-UCL.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0030552; F:cAMP binding; IEA:Ensembl.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IMP:MGI.
GO; GO:0006198; P:cAMP catabolic process; IDA:BHF-UCL.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0045822; P:negative regulation of heart contraction; IMP:BHF-UCL.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:1901898; P:negative regulation of relaxation of cardiac muscle; IMP:BHF-UCL.
GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0030814; P:regulation of cAMP metabolic process; IDA:CACAO.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL.
GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:BHF-UCL.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:BHF-UCL.
GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
Alternative splicing; cAMP; Cell membrane; Complete proteome;
Cytoplasm; Cytoskeleton; Hydrolase; Isopeptide bond; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 747 cAMP-specific 3',5'-cyclic
phosphodiesterase 4D.
/FTId=PRO_0000198815.
DOMAIN 325 654 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
NP_BIND 401 405 cAMP. {ECO:0000250}.
ACT_SITE 401 401 Proton donor. {ECO:0000250}.
METAL 405 405 Divalent metal cation 1. {ECO:0000250}.
METAL 441 441 Divalent metal cation 1. {ECO:0000250}.
METAL 442 442 Divalent metal cation 1. {ECO:0000250}.
METAL 442 442 Divalent metal cation 2. {ECO:0000250}.
METAL 559 559 Divalent metal cation 1. {ECO:0000250}.
BINDING 442 442 cAMP. {ECO:0000250}.
SITE 562 562 Binds AMP, but not cAMP. {ECO:0000250}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 163 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_012394.
VAR_SEQ 1 69 Missing (in isoform 9).
{ECO:0000303|Ref.2}.
/FTId=VSP_012395.
VAR_SEQ 70 91 RPTSLPLKILPLIAVTSADSSG -> MSIIMKPRSRSTSSL
RTTEAVC (in isoform 9).
{ECO:0000303|Ref.2}.
/FTId=VSP_012396.
VAR_SEQ 164 208 PFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINK
ATIT -> MKEQPSCAGTGHPSMAGYGRMAPFELAGGPVKR
LRTESSFPCLFA (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_012397.
CONFLICT 403 404 NI -> SR (in Ref. 5; AAA37368).
{ECO:0000305}.
SEQUENCE 747 AA; 84563 MW; 68402163664B3676 CRC64;
MERDTCDVLS RSKSASEETL HSCNEEEDPF RGMEPYLVRR LSSRSIQLPP LAFRQLEQAD
LRSESENIPR PTSLPLKILP LIAVTSADSS GFDVDNGTSA GRSPLDPMTS PGSGLILQAN
FVHSQRRESF LYRSDSDYDL SPKSMSRNSS IASDIHGDDL IVTPFAQVLA SLRTVRNNFA
ALTNLQDRAP SKRSPMCNQP SINKATITEE AYQKLASETL EELDWCLDQL ETLQTRHSVS
EMASNKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTQ KEKEKKKRPM
SQISGVKKLM HSSSLTNSCI PRFGVKTEQE DVLAKELEDV NKWGLHVFRI AELSGNRPLT
VIMHTIFQER DLLKTFKIPV DTLITYLMTL EDHYHADVAY HNNIHAADVV QSTHVLLSTP
ALEAVFTDLE ILAAIFASAI HDVDHPGVSN QFLINTNSEL ALMYNDSSVL ENHHLAVGFK
LLQEENCDIF QNLTKKQRQS LRKMVIDIVL ATDMSKHMNL LADLKTMVET KKVTSSGVLL
LDNYSDRIQV LQNMVHCADL SNPTKPLQLY RQWTDRIMEE FFRQGDRERE RGMEISPMCD
KHNASVEKSQ VGFIDYIVHP LWETWADLVH PDAQDILDTL EDNREWYQST IPQSPSPAPD
DQEEGRQGQT EKFQFELTLE EDCESDTEKD SGSQVEEDTS CSDSKTLCTQ DSESTEIPLD
EQVEEEAVAE EESQPETCVP DDCCPDT


Related products :

Catalog number Product name Quantity
EIAAB30321 cAMP-specific 3',5'-cyclic phosphodiesterase 4D,DPDE3,DPDE3,Homo sapiens,Human,PDE43,PDE4D
EIAAB30323 cAMP-specific 3',5'-cyclic phosphodiesterase 4D,DPDE3,Pde4d,Rat,Rattus norvegicus
EIAAB30322 cAMP-specific 3',5'-cyclic phosphodiesterase 4D,DPDE3,Mouse,Mus musculus,Pde4d
EIAAB30346 High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A,Pde7a,Rat,Rattus norvegicus,Rolipram-insensitive phosphodiesterase type 7
PDE4A_RAT Rat ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4A 96T
E0110m Rat ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4C 96T
ER300 cAMP-specific 3',5'-cyclic phosphodiesterase 4B Elisa Kit 96T
EH903 cAMP-specific 3',5'-cyclic phosphodiesterase 4B Elisa Kit 96T
TRML4_HUMAN Rat ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4C 96T
F154B_HUMAN Rat ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4C 96T
AL9A1_BOVIN Human ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4A 96T
E0044m Human ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4A 96T
E1658h Mouse ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4C 96T
UDB10_HUMAN Human ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4A 96T
PDE4A_MOUSE Mouse ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4A 96T
EIAAB30315 cAMP-specific 3',5'-cyclic phosphodiesterase 4A,Mouse,Mus musculus,Pde4a
E1630r Rat ELISA Kit FOR High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A 96T
EIAAB30320 cAMP-specific 3',5'-cyclic phosphodiesterase 4C,Mouse,Mus musculus,Pde4c
EIAAB30348 cAMP-specific 3',5'-cyclic phosphodiesterase 7B,Mouse,Mus musculus,Pde7b
E0823d Mouse ELISA Kit FOR High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A 96T
EIAAB30313 cAMP-specific 3',5'-cyclic phosphodiesterase 4A,DPDE2,Pde4a,Rat,Rattus norvegicus
EIAAB30317 cAMP-specific 3',5'-cyclic phosphodiesterase 4B,DPDE4,Pde4b,Rat,Rattus norvegicus
EIAAB30349 cAMP-specific 3',5'-cyclic phosphodiesterase 7B,Homo sapiens,Human,PDE7B
PDE4A_HUMAN ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4A; organism: Human; gene name: PDE4A 96T
PDE7B_HUMAN ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 7B; organism: Human; gene name: PDE7B 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur