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

Rho-associated protein kinase 2 (EC 2.7.11.1) (Rho-associated, coiled-coil-containing protein kinase 2) (Rho-associated, coiled-coil-containing protein kinase II) (ROCK-II) (RhoA-binding kinase 2) (p150 ROK-alpha) (ROKalpha) (p164 ROCK-2)

 ROCK2_RAT               Reviewed;        1388 AA.
Q62868;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 2.
12-SEP-2018, entry version 165.
RecName: Full=Rho-associated protein kinase 2;
EC=2.7.11.1;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase 2;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase II;
Short=ROCK-II;
AltName: Full=RhoA-binding kinase 2;
AltName: Full=p150 ROK-alpha;
Short=ROKalpha;
AltName: Full=p164 ROCK-2;
Name=Rock2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, INTERACTION
WITH RHOA, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=7493923; DOI=10.1074/jbc.270.49.29051;
Leung T., Manser E., Tan L., Lim L.;
"A novel serine/threonine kinase binding the Ras-related RhoA GTPase
which translocates the kinase to peripheral membranes.";
J. Biol. Chem. 270:29051-29054(1995).
[2]
FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH RHOA; RHOB AND RHOC,
MUTAGENESIS OF LYS-121, AND TISSUE SPECIFICITY.
PubMed=8816443; DOI=10.1128/MCB.16.10.5313;
Leung T., Chen X.-Q., Manser E., Lim L.;
"The p160 RhoA-binding kinase ROK alpha is a member of a kinase family
and is involved in the reorganization of the cytoskeleton.";
Mol. Cell. Biol. 16:5313-5327(1996).
[3]
FUNCTION, ROLE IN HYPERTENSION, AND INHIBITION BY Y-27632.
PubMed=9353125; DOI=10.1038/40187;
Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T.,
Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S.;
"Calcium sensitization of smooth muscle mediated by a Rho-associated
protein kinase in hypertension.";
Nature 389:990-994(1997).
[4]
INTERACTION WITH IRS1.
PubMed=11739394; DOI=10.1074/jbc.M110508200;
Begum N., Sandu O.A., Ito M., Lohmann S.M., Smolenski A.;
"Active Rho kinase (ROK-alpha) associates with insulin receptor
substrate-1 and inhibits insulin signaling in vascular smooth muscle
cells.";
J. Biol. Chem. 277:6214-6222(2002).
[5]
INTERACTION WITH RAF1.
PubMed=15753127; DOI=10.1083/jcb.200409162;
Ehrenreiter K., Piazzolla D., Velamoor V., Sobczak I., Small J.V.,
Takeda J., Leung T., Baccarini M.;
"Raf-1 regulates Rho signaling and cell migration.";
J. Cell Biol. 168:955-964(2005).
[6]
CLEAVAGE BY GRANZYME B.
PubMed=15699075; DOI=10.1084/jem.20031877;
Sebbagh M., Hamelin J., Bertoglio J., Solary E., Breard J.;
"Direct cleavage of ROCK II by granzyme B induces target cell membrane
blebbing in a caspase-independent manner.";
J. Exp. Med. 201:465-471(2005).
[7]
DOMAIN, PHOSPHORYLATION AT THR-414, AND MUTAGENESIS OF ASP-48;
LYS-121; THR-414 AND TRP-1170.
PubMed=19099536; DOI=10.1042/BJ20081376;
Couzens A.L., Saridakis V., Scheid M.P.;
"The hydrophobic motif of ROCK2 requires association with the N-
terminal extension for kinase activity.";
Biochem. J. 419:141-148(2009).
[8]
FUNCTION, INTERACTION WITH PPP1R12A, AND SUBCELLULAR LOCATION.
PubMed=19131646; DOI=10.1161/CIRCRESAHA.108.188524;
Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X.,
Surks H.K.;
"ROCK isoform regulation of myosin phosphatase and contractility in
vascular smooth muscle cells.";
Circ. Res. 104:531-540(2009).
[9]
FUNCTION IN PHOSPHORYLATION OF MYL9/MLC2 AND PPP1R12A.
PubMed=21457715; DOI=10.1016/j.febslet.2011.03.054;
Tan I., Lai J., Yong J., Li S.F., Leung T.;
"Chelerythrine perturbs lamellar actomyosin filaments by selective
inhibition of myotonic dystrophy kinase-related Cdc42-binding
kinase.";
FEBS Lett. 585:1260-1268(2011).
-!- FUNCTION: Protein kinase which is a key regulator of actin
cytoskeleton and cell polarity. Involved in regulation of smooth
muscle contraction, actin cytoskeleton organization, stress fiber
and focal adhesion formation, neurite retraction, cell adhesion
and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR,
DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM.
Phosphorylates SORL1 and IRF4. Acts as a negative regulator of
VEGF-induced angiogenic endothelial cell activation. Positively
regulates the activation of p42/MAPK1-p44/MAPK3 and of
p90RSK/RPS6KA1 during myogenic differentiation. Plays an important
role in the timely initiation of centrosome duplication. Inhibits
keratinocyte terminal differentiation. May regulate closure of the
eyelids and ventral body wall through organization of actomyosin
bundles. Plays a critical role in the regulation of spine and
synaptic properties in the hippocampus. Plays a role in placental
homeostasis during the perinatal period. Plays an important role
in generating the circadian rhythm of the aortic myofilament
Ca(2+) sensitivity and vascular contractility by modulating the
myosin light chain phosphorylation. {ECO:0000269|PubMed:19131646,
ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:7493923,
ECO:0000269|PubMed:8816443, ECO:0000269|PubMed:9353125}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-
27632.
-!- SUBUNIT: Homodimer (By similarity). Interacts with CHORDC1,
PPP1R12A, SORL1, EP300 and BRCA2 (By similarity). Interacts with
NPM1 and this interaction enhances its activity (By similarity).
Interacts with RHOA (activated by GTP), RHOB, RHOC and IRS1.
Interacts with RAF1. {ECO:0000250, ECO:0000269|PubMed:11739394,
ECO:0000269|PubMed:15753127, ECO:0000269|PubMed:19131646,
ECO:0000269|PubMed:7493923, ECO:0000269|PubMed:8816443}.
-!- INTERACTION:
P19105:MYL12A (xeno); NbExp=2; IntAct=EBI-1569209, EBI-354418;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000250}.
Note=Cytoplasmic, and associated with actin microfilaments and the
plasma membrane.
-!- TISSUE SPECIFICITY: Highly expressed in brain, lung, liver,
skeletal muscle, kidney and testis. {ECO:0000269|PubMed:8816443}.
-!- DOMAIN: An interaction between Thr-414 and Asp-48 is essential for
kinase activity and dimerization. {ECO:0000269|PubMed:19099536}.
-!- PTM: Autophosphorylated. Phosphorylation at Tyr-722 reduces its
binding to RHOA and is crucial for focal adhesion dynamics.
Dephosphorylation by PTPN11 stimulates its RHOA binding activity
(By similarity). {ECO:0000250}.
-!- PTM: Cleaved by granzyme B during apoptosis. This leads to
constitutive activation of the kinase and membrane blebbing.
-!- DISEASE: Note=May play a role in hypertension. ROCK-inhibitors
lower the blood pressure in spontaneous hypertensive, renal
hypertensive and deoxycorticosterone acetate-induced hypertensive
rats, but not in normal rats.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB37540.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; U38481; AAB37540.1; ALT_INIT; mRNA.
RefSeq; NP_037154.2; NM_013022.2.
UniGene; Rn.88642; -.
PDB; 2ROV; NMR; -; A=1151-1351.
PDB; 2ROW; NMR; -; A=1237-1320.
PDBsum; 2ROV; -.
PDBsum; 2ROW; -.
SMR; Q62868; -.
BioGrid; 247569; 1.
IntAct; Q62868; 5.
MINT; Q62868; -.
STRING; 10116.ENSRNOP00000006403; -.
BindingDB; Q62868; -.
ChEMBL; CHEMBL5490; -.
GuidetoPHARMACOLOGY; 1504; -.
iPTMnet; Q62868; -.
PhosphoSitePlus; Q62868; -.
PaxDb; Q62868; -.
PRIDE; Q62868; -.
GeneID; 25537; -.
KEGG; rno:25537; -.
CTD; 9475; -.
RGD; 3590; Rock2.
eggNOG; KOG0612; Eukaryota.
eggNOG; ENOG410XR1Q; LUCA.
HOGENOM; HOG000017259; -.
HOVERGEN; HBG053111; -.
InParanoid; Q62868; -.
KO; K17388; -.
EvolutionaryTrace; Q62868; -.
PRO; PR:Q62868; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; TAS:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0017048; F:Rho GTPase binding; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
GO; GO:0030261; P:chromosome condensation; TAS:RGD.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:ARUK-UCL.
GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
GO; GO:0032723; P:positive regulation of connective tissue growth factor production; IMP:ARUK-UCL.
GO; GO:1905205; P:positive regulation of connective tissue replacement; IMP:ARUK-UCL.
GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IMP:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0071559; P:response to transforming growth factor beta; IGI:ARUK-UCL.
GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
CDD; cd00029; C1; 1.
CDD; cd11638; HR1_ROCK2; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015008; Rho-bd_dom.
InterPro; IPR020684; ROCK1/ROCK2.
InterPro; IPR029878; ROCK2.
InterPro; IPR037311; ROCK2_HR1.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22988:SF28; PTHR22988:SF28; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08912; Rho_Binding; 1.
PIRSF; PIRSF037568; Rho_kinase; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS51860; REM_1; 1.
PROSITE; PS51859; RHO_BD; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Biological rhythms; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Zinc; Zinc-finger.
CHAIN 1 1388 Rho-associated protein kinase 2.
/FTId=PRO_0000086627.
DOMAIN 92 354 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 357 425 AGC-kinase C-terminal.
DOMAIN 497 573 REM-1. {ECO:0000255|PROSITE-
ProRule:PRU01207}.
DOMAIN 979 1047 RhoBD. {ECO:0000255|PROSITE-
ProRule:PRU01206}.
DOMAIN 1150 1349 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
NP_BIND 98 106 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 1260 1315 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 363 784 Interaction with PPP1R12A.
{ECO:0000269|PubMed:19131646}.
REGION 373 420 Interaction with NPM1. {ECO:0000250}.
REGION 979 1047 RHOA binding. {ECO:0000250}.
COILED 439 1024 {ECO:0000255}.
COILED 1052 1131 {ECO:0000255}.
ACT_SITE 214 214 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 121 121 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 1131 1132 Cleavage; by granzyme B.
MOD_RES 414 414 Phosphothreonine; by ROCK2.
{ECO:0000269|PubMed:19099536}.
MOD_RES 722 722 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:O75116}.
MOD_RES 1137 1137 Phosphoserine.
{ECO:0000250|UniProtKB:O75116}.
MOD_RES 1212 1212 Phosphothreonine.
{ECO:0000250|UniProtKB:O75116}.
MOD_RES 1362 1362 Phosphoserine.
{ECO:0000250|UniProtKB:O75116}.
MOD_RES 1374 1374 Phosphoserine.
{ECO:0000250|UniProtKB:O75116}.
MUTAGEN 48 48 D->A: Loss of kinase activity;
autophosphorylation and dimerization.
{ECO:0000269|PubMed:19099536}.
MUTAGEN 121 121 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:19099536,
ECO:0000269|PubMed:8816443}.
MUTAGEN 121 121 K->M: Loss of autophosphorylation.
{ECO:0000269|PubMed:19099536,
ECO:0000269|PubMed:8816443}.
MUTAGEN 414 414 T->A: Loss of kinase activity;
autophosphorylation and dimerization.
{ECO:0000269|PubMed:19099536}.
MUTAGEN 1170 1170 W->A: Increased activity and
autophosphorylation.
{ECO:0000269|PubMed:19099536}.
STRAND 1153 1158 {ECO:0000244|PDB:2ROV}.
STRAND 1163 1166 {ECO:0000244|PDB:2ROV}.
STRAND 1172 1178 {ECO:0000244|PDB:2ROV}.
STRAND 1181 1186 {ECO:0000244|PDB:2ROV}.
HELIX 1188 1192 {ECO:0000244|PDB:2ROV}.
STRAND 1197 1200 {ECO:0000244|PDB:2ROV}.
HELIX 1202 1204 {ECO:0000244|PDB:2ROV}.
STRAND 1205 1210 {ECO:0000244|PDB:2ROV}.
TURN 1213 1215 {ECO:0000244|PDB:2ROV}.
STRAND 1217 1219 {ECO:0000244|PDB:2ROV}.
TURN 1221 1223 {ECO:0000244|PDB:2ROV}.
HELIX 1224 1226 {ECO:0000244|PDB:2ROV}.
STRAND 1227 1232 {ECO:0000244|PDB:2ROV}.
STRAND 1234 1236 {ECO:0000244|PDB:2ROV}.
STRAND 1256 1258 {ECO:0000244|PDB:2ROW}.
STRAND 1261 1266 {ECO:0000244|PDB:2ROW}.
STRAND 1275 1281 {ECO:0000244|PDB:2ROW}.
STRAND 1284 1286 {ECO:0000244|PDB:2ROW}.
STRAND 1290 1296 {ECO:0000244|PDB:2ROW}.
STRAND 1299 1301 {ECO:0000244|PDB:2ROW}.
HELIX 1302 1307 {ECO:0000244|PDB:2ROW}.
TURN 1317 1319 {ECO:0000244|PDB:2ROW}.
STRAND 1325 1330 {ECO:0000244|PDB:2ROV}.
HELIX 1334 1347 {ECO:0000244|PDB:2ROV}.
SEQUENCE 1388 AA; 160387 MW; B23672CA8645067C CRC64;
MSRPPPTGKM PGAPEAAAGD GAGAGRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP
ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM
KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFCAFQ DDRYLYMVME YMPGGDLVNL
MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD
ETGMVHCDTA VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV
GTYSKIMDHK NSLCFPEDTE ISKHAKNLIC AFLTDREVRL GRNGVEEIKS ASFFKNDQWN
WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYFRENL
LLSDSPPCRE NDAIQTRKSE ESQEIQKKLY ALEEHLSSEV QAKEELEQKC KSINTRLEKT
AKELEEEITF RKNVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL
EDLKKRNQSS QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKTGKT
LLAKVELEKR QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKT TKARLADKNK
IYESIEEAKS EAMKEMEKKL LEERSLKQKV ENLLLEAEKR CSILDCDLKQ SQQKLNELLK
QKDVLNEDVR NLTLKIEQET QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN
LEKQNAELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK
KQDLQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE
LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDTQ EQLSKLKDEE ISAAAIKAQF
EKQLLTERTL KTQAVNKLAE IMNRKEPVKR GSDTDVRRKE KENRKLHMEL KSEREKLTQQ
MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGM DSSSIGSGPG
DAEPDDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EPEFPVEPVG EKSNYICHKG
HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECSRCHIKC HKDHMDKKEE IIAPCKVYYD
ISSAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR
QLAPNKPS


Related products :

Catalog number Product name Quantity
U1852r CLIA p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containi 96T
E1852r ELISA kit p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-co 96T
U1852r CLIA kit p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-con 96T
E1852r ELISA p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-contain 96T
E1852b ELISA Bos taurus,Bovine,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,ROCK2,ROCK-II 96T
U1852m CLIA kit Mouse,Mus musculus,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,Rock2,ROCK-II 96T
E1852m ELISA Mouse,Mus musculus,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,Rock2,ROCK-II 96T
E1852b ELISA kit Bos taurus,Bovine,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,ROCK2,ROCK-II 96T
U1852b CLIA kit Bos taurus,Bovine,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,ROCK2,ROCK-II 96T
U1852b CLIA Bos taurus,Bovine,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,ROCK2,ROCK-II 96T
E1852m ELISA kit Mouse,Mus musculus,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,Rock2,ROCK-II 96T
U1852m CLIA Mouse,Mus musculus,p164 ROCK-2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase II,Rock2,ROCK-II 96T
E1852h ELISA Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 96T
U1852h CLIA Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 96T
U1852h CLIA kit Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein ki 96T
E1852h ELISA kit Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein k 96T
EIAAB35680 Ac2-154,Liver regeneration-related protein LRRG199,p150 RhoA-binding kinase ROK beta,p160 ROCK-1,p160ROCK,Rat,Rattus norvegicus,Rho-associated protein kinase 1,Rho-associated, coiled-coil-containing p
EIAAB35679 Bos taurus,Bovine,p160 ROCK-1,p160ROCK,Rho-associated protein kinase 1,Rho-associated, coiled-coil-containing protein kinase 1,Rho-associated, coiled-coil-containing protein kinase I,ROCK1,ROCK-I
EIAAB35681 Mouse,Mus musculus,p160 ROCK-1,p160ROCK,Rho-associated protein kinase 1,Rho-associated, coiled-coil-containing protein kinase 1,Rho-associated, coiled-coil-containing protein kinase I,Rock1,ROCK-I
EIAAB35678 Homo sapiens,Human,p160 ROCK-1,p160ROCK,Renal carcinoma antigen NY-REN-35,Rho-associated protein kinase 1,Rho-associated, coiled-coil-containing protein kinase 1,Rho-associated, coiled-coil-containing
G8446 Rock-2 (Rho Associated Coiled Coil Containing Protein Kinase 2), Pig, ELISA Kit 96T
YHB2600Hu Human Rho-associated coiled-coil containing protein kinase 2,Rock-2 ELISA Kit 48T
E-EL-Ch1799 Chicken Rock-2 (Rho Associated Coiled Coil Containing Protein Kinase 2) ELISA Kit 96T
E0000Ca Canine Rho-associated coiled-coil containing protein kinase 2,Rock-2 ELISA Kit 96T
G8447 Rock-2 (Rho Associated Coiled Coil Containing Protein Kinase 2), Rabbit, ELISA Kit 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: 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

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