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 4C (EC 3.1.4.53) (DPDE1) (PDE21)

 PDE4C_HUMAN             Reviewed;         712 AA.
Q08493; B3KTC4; Q9UN44; Q9UN45; Q9UN46; Q9UPJ6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 2.
28-MAR-2018, entry version 158.
RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4C;
EC=3.1.4.53;
AltName: Full=DPDE1;
AltName: Full=PDE21;
Name=PDE4C; Synonyms=DPDE1;
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 PDE4C1).
TISSUE=Substantia nigra;
PubMed=7843419; DOI=10.1016/0014-5793(94)01460-I;
Engels P., Sullivan M., Mueller T., Luebbert H.;
"Molecular cloning and functional expression in yeast of a human cAMP-
specific phosphodiesterase subtype (PDE IV-C).";
FEBS Lett. 358:305-310(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PDE4C1; PDE4C2 AND
PDE4C3).
PubMed=10574328; DOI=10.1016/S0898-6568(99)00037-6;
Sullivan M., Olsen A.S., Houslay M.D.;
"Genomic organisation of the human cyclic AMP-specific
phosphodiesterase PDE4C gene and its chromosomal localisation to
19p13.1, between RAB3A and JUND.";
Cell. Signal. 11:735-742(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE4C1).
TISSUE=Tongue;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 462-712.
PubMed=8413254; DOI=10.1128/MCB.13.10.6558;
Bolger G., Michaeli T., Martins T., St John T., Steiner B.,
Rodgers L., Riggs M., Wigler M., Ferguson K.;
"A family of human phosphodiesterases homologous to the dunce learning
and memory gene product of Drosophila melanogaster are potential
targets for antidepressant drugs.";
Mol. Cell. Biol. 13:6558-6571(1993).
[7]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 306-663 IN COMPLEX WITH
METAL IONS, FUNCTION, AND COFACTOR.
PubMed=17727341; DOI=10.1042/BJ20070970;
Wang H., Peng M.-S., Chen Y., Geng J., Robinson H., Houslay M.D.,
Cai J., Ke H.;
"Structures of the four subfamilies of phosphodiesterase-4 provide
insight into the selectivity of their inhibitors.";
Biochem. J. 408:193-201(2007).
-!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
regulator of many important physiological processes.
{ECO:0000269|PubMed:17727341}.
-!- 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:0000269|PubMed:17727341};
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:17727341};
-!- ENZYME REGULATION: Inhibited by rolipram.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- SUBUNIT: Part of a complex containing AKAP5, ADCY5, ADCY6 and
PKD2. {ECO:0000250}.
-!- INTERACTION:
P26367:PAX6; NbExp=4; IntAct=EBI-12169289, EBI-747278;
P30626:SRI; NbExp=3; IntAct=EBI-10225541, EBI-750459;
-!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=PDE4C1;
IsoId=Q08493-1; Sequence=Displayed;
Name=PDE4C2;
IsoId=Q08493-2; Sequence=VSP_004575;
Name=PDE4C3;
IsoId=Q08493-3; Sequence=VSP_004574;
Name=PDE4C4;
IsoId=Q08493-4; Sequence=Not described;
Name=PDE4C5;
IsoId=Q08493-5; Sequence=Not described;
Name=PDE4C6;
IsoId=Q08493-6; Sequence=Not described;
Name=PDE4C7;
IsoId=Q08493-7; Sequence=Not described;
-!- TISSUE SPECIFICITY: Expressed in various tissues but not in cells
of the immune system.
-!- 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; Z46632; CAA86601.1; -; mRNA.
EMBL; AF157816; AAD47053.1; -; Genomic_DNA.
EMBL; AF157811; AAD47053.1; JOINED; Genomic_DNA.
EMBL; AF157814; AAD47053.1; JOINED; Genomic_DNA.
EMBL; AF157815; AAD47053.1; JOINED; Genomic_DNA.
EMBL; AF157816; AAD47054.1; -; Genomic_DNA.
EMBL; AF157812; AAD47054.1; JOINED; Genomic_DNA.
EMBL; AF157814; AAD47054.1; JOINED; Genomic_DNA.
EMBL; AF157815; AAD47054.1; JOINED; Genomic_DNA.
EMBL; AF157816; AAD47055.1; -; Genomic_DNA.
EMBL; AF157814; AAD47055.1; JOINED; Genomic_DNA.
EMBL; AF157815; AAD47055.1; JOINED; Genomic_DNA.
EMBL; AK095384; BAG53036.1; -; mRNA.
EMBL; AC005759; AAC83047.1; -; Genomic_DNA.
EMBL; CH471106; EAW84677.1; -; Genomic_DNA.
EMBL; L20968; AAA03591.1; -; mRNA.
CCDS; CCDS12373.1; -. [Q08493-1]
CCDS; CCDS42523.1; -. [Q08493-3]
CCDS; CCDS46016.1; -. [Q08493-2]
PIR; S71626; S71626.
RefSeq; NP_000914.2; NM_000923.5. [Q08493-1]
RefSeq; NP_001092288.1; NM_001098818.3. [Q08493-3]
RefSeq; NP_001092289.1; NM_001098819.3. [Q08493-2]
RefSeq; NP_001317101.1; NM_001330172.1. [Q08493-1]
RefSeq; XP_011526358.1; XM_011528056.2. [Q08493-2]
UniGene; Hs.132584; -.
PDB; 1LXU; Model; -; A=306-649.
PDB; 2QYM; X-ray; 1.90 A; A=306-663.
PDBsum; 1LXU; -.
PDBsum; 2QYM; -.
ProteinModelPortal; Q08493; -.
SMR; Q08493; -.
BioGrid; 111169; 1.
IntAct; Q08493; 6.
STRING; 9606.ENSP00000347689; -.
BindingDB; Q08493; -.
ChEMBL; CHEMBL291; -.
DrugBank; DB00201; Caffeine.
DrugBank; DB05219; Crisaborole.
DrugBank; DB00651; Dyphylline.
DrugBank; DB05266; Ibudilast.
DrugBank; DB01088; Iloprost.
DrugBank; DB01791; Piclamilast.
DrugBank; DB01656; Roflumilast.
GuidetoPHARMACOLOGY; 1302; -.
iPTMnet; Q08493; -.
PhosphoSitePlus; Q08493; -.
BioMuta; PDE4C; -.
DMDM; 20141263; -.
PaxDb; Q08493; -.
PeptideAtlas; Q08493; -.
PRIDE; Q08493; -.
Ensembl; ENST00000262805; ENSP00000262805; ENSG00000105650. [Q08493-3]
Ensembl; ENST00000355502; ENSP00000347689; ENSG00000105650. [Q08493-1]
Ensembl; ENST00000447275; ENSP00000402091; ENSG00000105650. [Q08493-2]
Ensembl; ENST00000594465; ENSP00000470210; ENSG00000105650. [Q08493-1]
Ensembl; ENST00000594617; ENSP00000469696; ENSG00000105650. [Q08493-1]
GeneID; 5143; -.
KEGG; hsa:5143; -.
UCSC; uc002nii.5; human. [Q08493-1]
CTD; 5143; -.
DisGeNET; 5143; -.
EuPathDB; HostDB:ENSG00000105650.21; -.
GeneCards; PDE4C; -.
HGNC; HGNC:8782; PDE4C.
HPA; HPA048975; -.
MIM; 600128; gene.
neXtProt; NX_Q08493; -.
OpenTargets; ENSG00000105650; -.
PharmGKB; PA264; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000118889; -.
HOVERGEN; HBG108239; -.
KO; K13293; -.
OMA; MCKTSLA; -.
OrthoDB; EOG091G06CD; -.
PhylomeDB; Q08493; -.
TreeFam; TF314638; -.
BRENDA; 3.1.4.53; 2681.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SIGNOR; Q08493; -.
UniPathway; UPA00762; UER00747.
ChiTaRS; PDE4C; human.
EvolutionaryTrace; Q08493; -.
GeneWiki; PDE4C; -.
GenomeRNAi; 5143; -.
PRO; PR:Q08493; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105650; -.
CleanEx; HS_PDE4C; -.
ExpressionAtlas; Q08493; baseline and differential.
Genevisible; Q08493; HS.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
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.
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; cAMP; Cell projection; Cilium;
Complete proteome; Hydrolase; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 712 cAMP-specific 3',5'-cyclic
phosphodiesterase 4C.
/FTId=PRO_0000198811.
DOMAIN 312 641 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
NP_BIND 388 392 cAMP. {ECO:0000250}.
ACT_SITE 388 388 Proton donor. {ECO:0000250}.
METAL 392 392 Divalent metal cation 1.
METAL 428 428 Divalent metal cation 1.
METAL 429 429 Divalent metal cation 1.
METAL 429 429 Divalent metal cation 2.
METAL 546 546 Divalent metal cation 1.
BINDING 429 429 cAMP. {ECO:0000250}.
BINDING 546 546 cAMP. {ECO:0000250}.
BINDING 597 597 cAMP. {ECO:0000250}.
SITE 549 549 Binds AMP, but not cAMP. {ECO:0000250}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UEI1}.
MOD_RES 641 641 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UEI1}.
VAR_SEQ 1 106 Missing (in isoform PDE4C2).
{ECO:0000305}.
/FTId=VSP_004575.
VAR_SEQ 1 81 MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIR
IQQRFYSDPDKSAGCRERDLSPRPELRKSRLSWPVSSCRR
-> MQGPPAPAPVPGPGSPRGSPRGSPGLFRKLLVNQSIRL
QRRFTVAHPLC (in isoform PDE4C3).
{ECO:0000305}.
/FTId=VSP_004574.
VARIANT 131 131 S -> L (in dbSNP:rs10413646).
/FTId=VAR_050473.
VARIANT 289 289 R -> Q (in dbSNP:rs34503849).
/FTId=VAR_050474.
VARIANT 344 344 R -> Q (in dbSNP:rs2229228).
/FTId=VAR_034374.
VARIANT 344 344 R -> W (in dbSNP:rs11879710).
/FTId=VAR_061497.
CONFLICT 204 204 K -> N (in Ref. 2; AAD47053/AAD47054).
{ECO:0000305}.
CONFLICT 211 211 D -> Y (in Ref. 2; AAD47053/AAD47054).
{ECO:0000305}.
CONFLICT 339 340 EL -> DV (in Ref. 1; CAA86601).
{ECO:0000305}.
CONFLICT 444 446 NSE -> K (in Ref. 4; AAC83047).
{ECO:0000305}.
CONFLICT 446 447 EL -> DV (in Ref. 1; CAA86601).
{ECO:0000305}.
HELIX 317 323 {ECO:0000244|PDB:2QYM}.
HELIX 324 326 {ECO:0000244|PDB:2QYM}.
HELIX 334 340 {ECO:0000244|PDB:2QYM}.
HELIX 345 356 {ECO:0000244|PDB:2QYM}.
HELIX 359 362 {ECO:0000244|PDB:2QYM}.
HELIX 367 379 {ECO:0000244|PDB:2QYM}.
STRAND 385 389 {ECO:0000244|PDB:2QYM}.
HELIX 390 404 {ECO:0000244|PDB:2QYM}.
HELIX 407 409 {ECO:0000244|PDB:2QYM}.
TURN 410 412 {ECO:0000244|PDB:2QYM}.
HELIX 415 427 {ECO:0000244|PDB:2QYM}.
TURN 428 431 {ECO:0000244|PDB:2QYM}.
HELIX 435 437 {ECO:0000244|PDB:2QYM}.
HELIX 456 467 {ECO:0000244|PDB:2QYM}.
HELIX 468 470 {ECO:0000244|PDB:2QYM}.
TURN 476 479 {ECO:0000244|PDB:2QYM}.
HELIX 482 497 {ECO:0000244|PDB:2QYM}.
HELIX 501 503 {ECO:0000244|PDB:2QYM}.
HELIX 504 516 {ECO:0000244|PDB:2QYM}.
HELIX 531 546 {ECO:0000244|PDB:2QYM}.
HELIX 549 551 {ECO:0000244|PDB:2QYM}.
HELIX 554 569 {ECO:0000244|PDB:2QYM}.
HELIX 600 603 {ECO:0000244|PDB:2QYM}.
HELIX 605 616 {ECO:0000244|PDB:2QYM}.
TURN 617 620 {ECO:0000244|PDB:2QYM}.
HELIX 621 630 {ECO:0000244|PDB:2QYM}.
SEQUENCE 712 AA; 79902 MW; 1932116C9CE0322C CRC64;
MENLGVGEGA EACSRLSRSR GRHSMTRAPK HLWRQPRRPI RIQQRFYSDP DKSAGCRERD
LSPRPELRKS RLSWPVSSCR RFDLENGLSC GRRALDPQSS PGLGRIMQAP VPHSQRRESF
LYRSDSDYEL SPKAMSRNSS VASDLHGEDM IVTPFAQVLA SLRTVRSNVA ALARQQCLGA
AKQGPVGNPS SSNQLPPAED TGQKLALETL DELDWCLDQL ETLQTRHSVG EMASNKFKRI
LNRELTHLSE TSRSGNQVSE YISRTFLDQQ TEVELPKVTA EEAPQPMSRI SGLHGLCHSA
SLSSATVPRF GVQTDQEEQL AKELEDTNKW GLDVFKVAEL SGNRPLTAII FSIFQERDLL
KTFQIPADTL ATYLLMLEGH YHANVAYHNS LHAADVAQST HVLLATPALE AVFTDLEILA
ALFASAIHDV DHPGVSNQFL INTNSELALM YNDASVLENH HLAVGFKLLQ AENCDIFQNL
SAKQRLSLRR MVIDMVLATD MSKHMNLLAD LKTMVETKKV TSLGVLLLDN YSDRIQVLQN
LVHCADLSNP TKPLPLYRQW TDRIMAEFFQ QGDRERESGL DISPMCDKHT ASVEKSQVGF
IDYIAHPLWE TWADLVHPDA QDLLDTLEDN REWYQSKIPR SPSDLTNPER DGPDRFQFEL
TLEEAEEEDE EEEEEGEETA LAKEALELPD TELLSPEAGP DPGDLPLDNQ RT


Related products :

Catalog number Product name Quantity
EIAAB30318 cAMP-specific 3',5'-cyclic phosphodiesterase 4C,DPDE1,DPDE1,Homo sapiens,Human,PDE21,PDE4C
EIAAB30319 cAMP-specific 3',5'-cyclic phosphodiesterase 4C,DPDE1,Dpde1,Pde4c,Rat,Rattus norvegicus
EIAAB30346 High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A,Pde7a,Rat,Rattus norvegicus,Rolipram-insensitive phosphodiesterase type 7
ER300 cAMP-specific 3',5'-cyclic phosphodiesterase 4B Elisa Kit 96T
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
TRML4_HUMAN Rat ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4C 96T
EH903 cAMP-specific 3',5'-cyclic phosphodiesterase 4B Elisa Kit 96T
F154B_HUMAN Rat ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4C 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
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
PDE4A_MOUSE Mouse ELISA Kit FOR cAMP-specific 3',5'-cyclic phosphodiesterase 4A 96T
E1630r Rat ELISA Kit FOR High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A 96T
EIAAB30348 cAMP-specific 3',5'-cyclic phosphodiesterase 7B,Mouse,Mus musculus,Pde7b
EIAAB30315 cAMP-specific 3',5'-cyclic phosphodiesterase 4A,Mouse,Mus musculus,Pde4a
EIAAB30320 cAMP-specific 3',5'-cyclic phosphodiesterase 4C,Mouse,Mus musculus,Pde4c
EIAAB30317 cAMP-specific 3',5'-cyclic phosphodiesterase 4B,DPDE4,Pde4b,Rat,Rattus norvegicus
EIAAB30322 cAMP-specific 3',5'-cyclic phosphodiesterase 4D,DPDE3,Mouse,Mus musculus,Pde4d
EIAAB30313 cAMP-specific 3',5'-cyclic phosphodiesterase 4A,DPDE2,Pde4a,Rat,Rattus norvegicus
E0823d Mouse ELISA Kit FOR High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A 96T
EIAAB30323 cAMP-specific 3',5'-cyclic phosphodiesterase 4D,DPDE3,Pde4d,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


 

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