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

cGMP-dependent protein kinase 1 (cGK 1) (cGK1) (EC 2.7.11.12) (cGMP-dependent protein kinase I) (cGKI)

 KGP1_BOVIN              Reviewed;         671 AA.
P00516; P21136;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 168.
RecName: Full=cGMP-dependent protein kinase 1;
Short=cGK 1;
Short=cGK1;
EC=2.7.11.12;
AltName: Full=cGMP-dependent protein kinase I;
Short=cGKI;
Name=PRKG1; Synonyms=PRKG1B, PRKGR1A, PRKGR1B;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
PubMed=2546820; DOI=10.1016/0014-5793(89)81453-X;
Wernet W., Flockerzi V., Hofmann F.;
"The cDNA of the two isoforms of bovine cGMP-dependent protein
kinase.";
FEBS Lett. 251:191-196(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
TISSUE=Testis;
PubMed=9099696; DOI=10.1074/jbc.272.16.10522;
Ruth P., Pfeifer A., Kamm S., Klatt P., Dostmann W.R., Hofmann F.;
"Identification of the amino acid sequences responsible for high
affinity activation of cGMP kinase Ialpha.";
J. Biol. Chem. 272:10522-10528(1997).
[3]
PROTEIN SEQUENCE OF 2-18; 90-375 AND 408-671, AND ACETYLATION AT
SER-2.
PubMed=6091741; DOI=10.1021/bi00313a030;
Takio K., Wade R.D., Smith S.B., Krebs E.G., Walsh K.A., Titani K.;
"Guanosine cyclic 3',5'-phosphate dependent protein kinase, a chimeric
protein homologous with two separate protein families.";
Biochemistry 23:4207-4218(1984).
[4]
PROTEIN SEQUENCE OF 14-105 (ISOFORM ALPHA), PHOSPHORYLATION AT THR-59,
AND BLOCKAGE OF N-TERMINUS.
TISSUE=Lung;
PubMed=6304091;
Takio K., Smith S.B., Walsh K.A., Krebs E.G., Titani K.;
"Amino acid sequence around a 'hinge' region and its
'autophosphorylation' site in bovine lung cGMP-dependent protein
kinase.";
J. Biol. Chem. 258:5531-5536(1983).
[5]
PROTEIN SEQUENCE OF 63-75 (ISOFORM BETA).
TISSUE=Aorta;
PubMed=2537306;
Wolfe L., Francis S.H., Corbin J.D.;
"Properties of a cGMP-dependent monomeric protein kinase from bovine
aorta.";
J. Biol. Chem. 264:4157-4162(1989).
[6]
PROTEIN SEQUENCE OF 374-410, AND ATP-BINDING AT LYS-390.
PubMed=6274862;
Hashimoto E., Takio K., Krebs E.G.;
"Amino acid sequence at the ATP-binding site of cGMP-dependent protein
kinase.";
J. Biol. Chem. 257:727-733(1982).
[7]
PROTEIN SEQUENCE OF 79-82 (ISOFORM ALPHA), AND CHARACTERIZATION.
PubMed=2822399; DOI=10.1111/j.1432-1033.1987.tb13395.x;
Heil W.G., Landgraf W., Hofmann F.;
"A catalytically active fragment of cGMP-dependent protein kinase.
Occupation of its cGMP-binding sites does not affect its
phosphotransferase activity.";
Eur. J. Biochem. 168:117-121(1987).
[8]
TISSUE SPECIFICITY.
PubMed=1325910; DOI=10.1111/j.1432-1033.1992.tb17209.x;
Keilbach A., Ruth P., Hofmann F.;
"Detection of cGMP dependent protein kinase isozymes by specific
antibodies.";
Eur. J. Biochem. 208:467-473(1992).
[9]
INTERACTION WITH MRVI1.
PubMed=10724174; DOI=10.1038/35004606;
Schlossmann J., Ammendola A., Ashman K., Zong X., Huber A.,
Neubauer G., Wang G.-X., Allescher H.-D., Korth M., Wilm M.,
Hofmann F., Ruth P.;
"Regulation of intracellular calcium by a signalling complex of IRAG,
IP3 receptor and cGMP kinase Ibeta.";
Nature 404:197-201(2000).
[10]
INTERACTION WITH MRVI1.
PubMed=11309393; DOI=10.1074/jbc.M101530200;
Ammendola A., Geiselhoeringer A., Hofmann F., Schlossmann J.;
"Molecular determinants of the interaction between the inositol 1,4,5-
trisphosphate receptor-associated cGMP kinase substrate (IRAG) and
cGMP kinase Ibeta.";
J. Biol. Chem. 276:24153-24159(2001).
[11]
SUBUNIT.
PubMed=12480535; DOI=10.1016/S0006-291X(02)02799-7;
Koller A., Schlossmann J., Ashman K., Uttenweiler-Joseph S., Ruth P.,
Hofmann F.;
"Association of phospholamban with a cGMP kinase signaling complex.";
Biochem. Biophys. Res. Commun. 300:155-160(2003).
[12]
INTERACTION WITH MRVI1.
PubMed=16166082; DOI=10.1074/jbc.M507021200;
Casteel D.E., Boss G.R., Pilz R.B.;
"Identification of the interface between cGMP-dependent protein kinase
Ibeta and its interaction partners TFII-I and IRAG reveals a common
interaction motif.";
J. Biol. Chem. 280:38211-38218(2005).
[13]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 79-356 IN COMPLEX WITH CAMP.
PubMed=21893290; DOI=10.1016/j.str.2011.06.012;
Osborne B.W., Wu J., McFarland C.J., Nickl C.K., Sankaran B.,
Casteel D.E., Woods V.L. Jr., Kornev A.P., Taylor S.S., Dostmann W.R.;
"Crystal structure of cGMP-dependent protein kinase reveals novel site
of interchain communication.";
Structure 19:1317-1327(2011).
-!- FUNCTION: Serine/threonine protein kinase that acts as key
mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP
binding activates PRKG1, which phosphorylates serines and
threonines on many cellular proteins. Numerous protein targets for
PRKG1 phosphorylation are implicated in modulating cellular
calcium, but the contribution of each of these targets may vary
substantially among cell types. Proteins that are phosphorylated
by PRKG1 regulate platelet activation and adhesion, smooth muscle
contraction, cardiac function, gene expression, feedback of the
NO-signaling pathway, and other processes involved in several
aspects of the CNS like axon guidance, hippocampal and cerebellar
learning, circadian rhythm and nociception. Smooth muscle
relaxation is mediated through lowering of intracellular free
calcium, by desensitization of contractile proteins to calcium,
and by decrease in the contractile state of smooth muscle or in
platelet activation. Regulates intracellular calcium levels via
several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-
induced Ca(2+) release from intracellular stores, phosphorylation
of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels,
which leads to increased opening of this channel. PRKG1
phosphorylates the canonical transient receptor potential channel
(TRPC) family which inactivates the associated inward calcium
current. Another mode of action of NO/cGMP/PKGI signaling involves
PKGI-mediated inactivation of the Ras homolog gene family member A
(RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this
protein in myriad processes: regulation of RHOA translocation;
decreasing contraction; controlling vesicle trafficking, reduction
of myosin light chain phosphorylation resulting in vasorelaxation.
Activation of PRKG1 by NO signaling alters also gene expression in
a number of tissues. In smooth muscle cells, increased cGMP and
PRKG1 activity influence expression of smooth muscle-specific
contractile proteins, levels of proteins in the NO/cGMP signaling
pathway, down-regulation of the matrix proteins osteopontin and
thrombospondin-1 to limit smooth muscle cell migration and
phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP)
functions in platelets and smooth muscle (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.12;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.12;
-!- ACTIVITY REGULATION: In the absence of cGMP, PRKG1 activity is
suppressed by autoinhibitory contacts. {ECO:0000250}.
-!- SUBUNIT: Isoform alpha: parallel homodimer or heterodimer and also
heterotetramer. Interacts directly with PPP1R12A. Non-covalent
dimer of dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This
interaction targets PRKG1 to stress fibers to mediate smooth
muscle cell relaxation and vasodilation in responses to rises in
cGMP (By similarity). Isoform beta: antiparallel homodimer. Part
of cGMP kinase signaling complex at least composed of ACTA2/alpha-
actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1.
Interacts with MRVI1 (By similarity). Forms a stable complex with
ITPR1, MRVI1, and isoform beta of PRKG1 (By similarity). Interacts
with TRPC7 (via ankyrin repeat domain) (By similarity). Isoform
alpha interacts with RGS2 (By similarity). Interacts with GTF2I
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalized
with TRPC7 in the plasma membrane. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha; Synonyms=CGK1-alpha;
IsoId=P00516-1; Sequence=Displayed;
Name=Beta; Synonyms=CGK1-beta;
IsoId=P00516-2, P21136-1;
Sequence=VSP_038713;
-!- TISSUE SPECIFICITY: High concentrations are detected in various
smooth muscle: lung, rumen, trachea, aorta, uterus and stomach.
Isoform alpha is expressed predominantly in heart, cerebellum and
lung, whereas the beta isoform is expressed in high concentrations
in trachea, aorta, stomach and uterus.
{ECO:0000269|PubMed:1325910}.
-!- DOMAIN: Composed of an N-terminal leucine-zipper domain followed
by an autoinhibitory domain, which mediate homodimer formation and
inhibit kinase activity, respectively. Next, two cGMP-binding
domains are followed by the catalytic domain at the C-terminus.
Binding of cGMP to cGMP-binding domains results in a
conformational change that activates kinase activity by removing
the autoinhibitory domain from the catalytic cleft leaving the
catalytic domain free to phosphorylate downstream substrates.
Isoforms alpha and beta have identical cGMP-binding and catalytic
domains but differ in their leucine zipper and autoinhibitory
sequences and therefore differ in their dimerization substrates
and kinase enzyme activity.
-!- DOMAIN: Heterotetramerization is mediated by the interaction
between a coiled-coil of PRKG1 and the leucine/isoleucine zipper
of PPP1R12A/MBS, the myosin-binding subunit of the myosin
phosphatase. {ECO:0000250}.
-!- PTM: Autophosphorylation increases kinase activity. {ECO:0000250}.
-!- PTM: 65 kDa monomer is produced by proteolytic cleavage.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cGMP subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X16086; CAA34214.1; -; mRNA.
EMBL; X54289; CAA38184.1; -; mRNA.
EMBL; Y08961; CAA70155.1; -; mRNA.
PIR; A00619; OKBOG.
PIR; S05035; S05035.
RefSeq; NP_776861.1; NM_174436.2. [P00516-1]
RefSeq; XP_005225410.1; XM_005225353.2. [P00516-2]
UniGene; Bt.63035; -.
UniGene; Bt.9; -.
PDB; 3SHR; X-ray; 2.50 A; A/B=79-356.
PDBsum; 3SHR; -.
ProteinModelPortal; P00516; -.
SMR; P00516; -.
BioGrid; 159293; 2.
CORUM; P00516; -.
DIP; DIP-59143N; -.
IntAct; P00516; 3.
BindingDB; P00516; -.
ChEMBL; CHEMBL3183; -.
iPTMnet; P00516; -.
PRIDE; P00516; -.
Ensembl; ENSBTAT00000024490; ENSBTAP00000024490; ENSBTAG00000018404. [P00516-1]
GeneID; 282004; -.
KEGG; bta:282004; -.
CTD; 5592; -.
VGNC; VGNC:33340; PRKG1.
GeneTree; ENSGT00940000154704; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG006211; -.
InParanoid; P00516; -.
KO; K07376; -.
BRENDA; 2.7.11.12; 908.
Reactome; R-BTA-392517; Rap1 signalling.
Reactome; R-BTA-418457; cGMP effects.
Proteomes; UP000009136; Chromosome 26.
Bgee; ENSBTAG00000018404; Expressed in 10 organ(s), highest expression level in brain.
ExpressionAtlas; P00516; baseline and differential.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0004692; F:cGMP-dependent protein kinase activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
CDD; cd00038; CAP_ED; 2.
CDD; cd05572; STKc_cGK; 1.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR039811; cAMP/cGMP-dep_PK.
InterPro; IPR002374; cGMP_dep_kinase.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR031831; PKcGMP_CC.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR035014; STKc_cGK.
PANTHER; PTHR24353; PTHR24353; 1.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF16808; PKcGMP_CC; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
PRINTS; PR00104; CGMPKINASE.
SMART; SM00100; cNMP; 2.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF51206; SSF51206; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00888; CNMP_BINDING_1; 2.
PROSITE; PS00889; CNMP_BINDING_2; 2.
PROSITE; PS50042; CNMP_BINDING_3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
ATP-binding; cGMP; cGMP-binding; Coiled coil; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6091741}.
CHAIN 2 671 cGMP-dependent protein kinase 1.
/FTId=PRO_0000086114.
DOMAIN 360 619 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 620 671 AGC-kinase C-terminal.
NP_BIND 167 170 cAMP or cGMP 1. {ECO:0000244|PDB:3SHR,
ECO:0000269|PubMed:21893290}.
NP_BIND 177 178 cAMP or cGMP 1. {ECO:0000244|PDB:3SHR,
ECO:0000269|PubMed:21893290}.
NP_BIND 291 294 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 301 302 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 366 374 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 102 Required for dimerization.
REGION 9 44 Leucine-zipper.
REGION 50 75 Autoinhibitory domain. {ECO:0000250}.
REGION 103 220 cGMP-binding, high affinity.
{ECO:0000250}.
REGION 221 341 cGMP-binding, low affinity.
{ECO:0000250}.
COILED 2 59 {ECO:0000250}.
ACT_SITE 484 484 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 282 282 cGMP 2. {ECO:0000250|UniProtKB:Q13976}.
BINDING 336 336 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
BINDING 390 390 ATP.
SITE 78 79 Cleavage.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:6091741}.
MOD_RES 59 59 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:6304091}.
MOD_RES 515 515 Phosphothreonine.
{ECO:0000250|UniProtKB:P0C605}.
DISULFID 43 43 Interchain.
VAR_SEQ 1 89 MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLH
KCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFR
KFTKSER -> MGTLRDLQYALQEKIEELRQRDALIDELEL
ELDQKDELIQKLQNELDKYRSVIRPATQQAQKQSASTLQGE
PRTKRQAISAEPTAFDIQDLSHVTLPFYPKSPQ (in
isoform Beta).
{ECO:0000303|PubMed:2546820,
ECO:0000303|PubMed:9099696}.
/FTId=VSP_038713.
HELIX 88 99 {ECO:0000244|PDB:3SHR}.
TURN 102 106 {ECO:0000244|PDB:3SHR}.
HELIX 109 118 {ECO:0000244|PDB:3SHR}.
STRAND 120 124 {ECO:0000244|PDB:3SHR}.
STRAND 129 131 {ECO:0000244|PDB:3SHR}.
STRAND 140 146 {ECO:0000244|PDB:3SHR}.
STRAND 148 152 {ECO:0000244|PDB:3SHR}.
STRAND 155 160 {ECO:0000244|PDB:3SHR}.
STRAND 165 167 {ECO:0000244|PDB:3SHR}.
HELIX 170 172 {ECO:0000244|PDB:3SHR}.
TURN 173 175 {ECO:0000244|PDB:3SHR}.
STRAND 179 185 {ECO:0000244|PDB:3SHR}.
STRAND 187 192 {ECO:0000244|PDB:3SHR}.
HELIX 194 216 {ECO:0000244|PDB:3SHR}.
HELIX 220 224 {ECO:0000244|PDB:3SHR}.
HELIX 227 233 {ECO:0000244|PDB:3SHR}.
TURN 234 236 {ECO:0000244|PDB:3SHR}.
STRAND 238 242 {ECO:0000244|PDB:3SHR}.
STRAND 247 249 {ECO:0000244|PDB:3SHR}.
STRAND 257 270 {ECO:0000244|PDB:3SHR}.
STRAND 273 275 {ECO:0000244|PDB:3SHR}.
STRAND 279 285 {ECO:0000244|PDB:3SHR}.
HELIX 292 295 {ECO:0000244|PDB:3SHR}.
STRAND 296 300 {ECO:0000244|PDB:3SHR}.
STRAND 302 317 {ECO:0000244|PDB:3SHR}.
HELIX 318 325 {ECO:0000244|PDB:3SHR}.
HELIX 333 354 {ECO:0000244|PDB:3SHR}.
SEQUENCE 671 AA; 76419 MW; 9FE7A48422DA9CDF CRC64;
MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR
AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY
PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT
VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET
HYENGEYIIR QGARGDTFFI ISKGKVNVTR EDSPNEDPVF LRTLGKGDWF GEKALQGEDV
RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA FFANLKLSDF
NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF
IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI
IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD
YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS
ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD SFPEDNDEPP
PDDNSGWDID F


Related products :

Catalog number Product name Quantity
82801-73-8 cGMP Dependent kinase inhibitor peptid cGMP Dependent Kina 1g
KGP2_RAT Rat ELISA Kit FOR cGMP-dependent protein kinase 2 96T
CSB-EL018716RA Rat cGMP-dependent protein kinase 2(PRKG2) ELISA kit 96T
KGP2_HUMAN Human ELISA Kit FOR cGMP-dependent protein kinase 2 96T
EH3652 Protein Kinase, cGMP Dependent Type I Elisa Kit 96T
CSB-EL018716MO Mouse cGMP-dependent protein kinase 2(PRKG2) ELISA kit 96T
CSB-EL018715MO Mouse cGMP-dependent protein kinase 1(PRKG1) ELISA kit 96T
CSB-EL018715HU Human cGMP-dependent protein kinase 1(PRKG1) ELISA kit 96T
E97314Hu ELISA Kit for Protein Kinase, cGMP Dependent Type I (PRKG1) 96T/Kit
E13242h Human Protein Kinase, cGMP Dependent Type II ELISA 96T
PRKRA PRKG1 Gene protein kinase, cGMP-dependent, type I
PRKRIP1 PRKG2 Gene protein kinase, cGMP-dependent, type II
G0871 PRKG1 (Protein Kinase, cGMP Dependent Type I), Pig, ELISA Kit 96T
CSB-EL018715BO Bovine cGMP-dependent protein kinase 1(PRKG1) ELISA kit 96T
CSB-EL018716HU Human cGMP-dependent protein kinase 2(PRKG2) ELISA kit 96T
CSB-EL018716RA Rat cGMP-dependent protein kinase 2(PRKG2) ELISA kit SpeciesRat 96T
CSB-EL018716HU Human cGMP-dependent protein kinase 2(PRKG2) ELISA kit SpeciesHuman 96T
G0868 PRKG1 (Protein Kinase, cGMP Dependent Type I), Guinea Pig, ELISA Kit 96T
UB-E05051 Human Protein Kinase, cGMP Dependent Type I(PRKG1)ELISA Kit 96T
CSB-EL018715RB Rabbit cGMP-dependent protein kinase 1(PRKG1) ELISA kit SpeciesRabbit 96T
CSB-EL018716MO Mouse cGMP-dependent protein kinase 2(PRKG2) ELISA kit SpeciesMouse 96T
QY-E05051 Human Protein Kinase, cGMP Dependent Type I(PRKG1)ELISA Kit 96T
CSB-EL018715MO Mouse cGMP-dependent protein kinase 1(PRKG1) ELISA kit SpeciesMouse 96T
G0872 PRKG1 (Protein Kinase, cGMP Dependent Type I), Rabbit, ELISA Kit 96T
CSB-EL018715HU Human cGMP-dependent protein kinase 1(PRKG1) ELISA kit SpeciesHuman 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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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