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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) (p164 ROCK-2)

 ROCK2_MOUSE             Reviewed;        1388 AA.
P70336; A5XDA7; Q8BR64; Q8CBR0;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
30-AUG-2017, entry version 167.
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=p164 ROCK-2;
Name=Rock2;
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 1), AND TISSUE SPECIFICITY.
PubMed=8772201; DOI=10.1016/0014-5793(96)00811-3;
Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K.,
Narumiya S.;
"ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil
forming protein serine/threonine kinase in mice.";
FEBS Lett. 392:189-193(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1144 (ISOFORM 2), PHOSPHORYLATION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=17606625; DOI=10.1128/MCB.01735-06;
Pelosi M., Marampon F., Zani B.M., Prudente S., Perlas E., Caputo V.,
Cianetti L., Berno V., Narumiya S., Kang S.W., Musaro A.,
Rosenthal N.;
"ROCK2 and its alternatively spliced isoform ROCK2m positively control
the maturation of the myogenic program.";
Mol. Cell. Biol. 27:6163-6176(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 633-1388 AND 677-1388.
STRAIN=C57BL/6J; TISSUE=Brain, and Urinary bladder;
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]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12832488; DOI=10.1128/MCB.23.14.5043-5055.2003;
Thumkeo D., Keel J., Ishizaki T., Hirose M., Nonomura K., Oshima H.,
Oshima M., Taketo M.M., Narumiya S.;
"Targeted disruption of the mouse rho-associated kinase 2 gene results
in intrauterine growth retardation and fetal death.";
Mol. Cell. Biol. 23:5043-5055(2003).
[5]
DISRUPTION PHENOTYPE.
PubMed=15753128; DOI=10.1083/jcb.200411179;
Shimizu Y., Thumkeo D., Keel J., Ishizaki T., Oshima H., Oshima M.,
Noda Y., Matsumura F., Taketo M.M., Narumiya S.;
"ROCK-I regulates closure of the eyelids and ventral body wall by
inducing assembly of actomyosin bundles.";
J. Cell Biol. 168:941-953(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]
FUNCTION.
PubMed=19181962; DOI=10.1152/ajpheart.01038.2008;
Kroll J., Epting D., Kern K., Dietz C.T., Feng Y., Hammes H.P.,
Wieland T., Augustin H.G.;
"Inhibition of Rho-dependent kinases ROCK I/II activates VEGF-driven
retinal neovascularization and sprouting angiogenesis.";
Am. J. Physiol. 296:H893-H899(2009).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18718479; DOI=10.1016/j.neuropharm.2008.07.031;
Zhou Z., Meng Y., Asrar S., Todorovski Z., Jia Z.;
"A critical role of Rho-kinase ROCK2 in the regulation of spine and
synaptic function.";
Neuropharmacology 56:81-89(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137 AND SER-1374, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[10]
FUNCTION.
PubMed=20697158; DOI=10.1172/JCI42856;
Biswas P.S., Gupta S., Chang E., Song L., Stirzaker R.A., Liao J.K.,
Bhagat G., Pernis A.B.;
"Phosphorylation of IRF4 by ROCK2 regulates IL-17 and IL-21 production
and the development of autoimmunity in mice.";
J. Clin. Invest. 120:3280-3295(2010).
[11]
FUNCTION, AND INDUCTION.
PubMed=23172836; DOI=10.1161/CIRCULATIONAHA.112.135608;
Saito T., Hirano M., Ide T., Ichiki T., Koibuchi N., Sunagawa K.,
Hirano K.;
"Pivotal role of Rho-associated kinase 2 in generating the intrinsic
circadian rhythm of vascular contractility.";
Circulation 127:104-114(2013).
-!- 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:12832488,
ECO:0000269|PubMed:18718479, ECO:0000269|PubMed:19181962,
ECO:0000269|PubMed:20697158, ECO:0000269|PubMed:23172836}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by RHOA binding. Inhibited by Y-27632
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with RHOA (activated by GTP),
CHORDC1, IRS1, RHOB, RHOC, PPP1R12A, SORL1, EP300 and BRCA2.
Interacts with NPM1 and this interaction enhances its activity.
Interacts with RAF1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: 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. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Cell membrane;
Peripheral membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70336-1; Sequence=Displayed;
Name=2; Synonyms=ROCK2m;
IsoId=P70336-2; Sequence=VSP_041818, VSP_041819;
-!- TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, liver,
stomach, spleen, kidney, testis, muscle, embryo and placenta.
Isoform 2 is expressed predominantly in the skeletal muscle.
{ECO:0000269|PubMed:17606625, ECO:0000269|PubMed:8772201}.
-!- INDUCTION: Expression oscillates in a circadian manner in the
aorta. {ECO:0000269|PubMed:23172836}.
-!- DOMAIN: An interaction between Thr-414 and Asp-48 is essential for
kinase activity and dimerization. {ECO:0000250}.
-!- 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.
-!- DISRUPTION PHENOTYPE: Mice exhibit both EOB (eyes open at birth)
and omphalocele phenotypes as a result of disorganization of
actomyosin cables in the eyelid epithelium and defective actin
assembly in the umbilical ring. Mice are impaired in both basal
synaptic transmission and hippocampal long-term potentiation
(LTP). Embryos manifest extensive thrombus formation in the
placenta, resulting in placental dysfunction, intrauterine growth
retardation, and fetal death. {ECO:0000269|PubMed:12832488,
ECO:0000269|PubMed:15753128, ECO:0000269|PubMed:18718479}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
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EMBL; U58513; AAC53133.1; -; mRNA.
EMBL; DQ864977; ABI75318.1; -; mRNA.
EMBL; AK045517; BAC32403.1; -; mRNA.
EMBL; AK035509; BAC29084.1; -; mRNA.
CCDS; CCDS36410.1; -. [P70336-1]
PIR; S74245; S74245.
RefSeq; NP_033098.2; NM_009072.2.
UniGene; Mm.276024; -.
ProteinModelPortal; P70336; -.
SMR; P70336; -.
BioGrid; 202951; 7.
IntAct; P70336; 5.
MINT; MINT-4132887; -.
STRING; 10090.ENSMUSP00000020904; -.
iPTMnet; P70336; -.
PhosphoSitePlus; P70336; -.
SwissPalm; P70336; -.
EPD; P70336; -.
MaxQB; P70336; -.
PaxDb; P70336; -.
PeptideAtlas; P70336; -.
PRIDE; P70336; -.
GeneID; 19878; -.
KEGG; mmu:19878; -.
UCSC; uc007ncg.1; mouse. [P70336-2]
CTD; 9475; -.
MGI; MGI:107926; Rock2.
eggNOG; KOG0612; Eukaryota.
eggNOG; ENOG410XR1Q; LUCA.
HOGENOM; HOG000017259; -.
HOVERGEN; HBG053111; -.
InParanoid; P70336; -.
KO; K17388; -.
PhylomeDB; P70336; -.
PRO; PR:P70336; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031616; C:spindle pole centrosome; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0017048; F:Rho GTPase binding; IEA:InterPro.
GO; GO:0072518; F:Rho-dependent protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:MGI.
GO; GO:0051298; P:centrosome duplication; ISO:MGI.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
GO; GO:0090002; P:establishment of protein localization to plasma membrane; ISO:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:MGI.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
GO; GO:0001843; P:neural tube closure; IGI:MGI.
GO; GO:0010825; P:positive regulation of centrosome duplication; IMP:MGI.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
GO; GO:0045616; P:regulation of keratinocyte differentiation; ISO:MGI.
GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; ISO:MGI.
CDD; cd00029; C1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH_dom-like.
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; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22988:SF40; PTHR22988:SF40; 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; SSF50729; SSF50729; 2.
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; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Alternative splicing; 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_0000086626.
DOMAIN 92 354 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 357 425 AGC-kinase C-terminal.
REPEAT 475 559 REM.
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:0000250}.
REGION 373 420 Interaction with NPM1. {ECO:0000250}.
REGION 979 1047 RHOA binding. {ECO:0000250}.
COILED 439 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:0000250|UniProtKB:Q62868}.
MOD_RES 722 722 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:O75116}.
MOD_RES 1137 1137 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1212 1212 Phosphothreonine.
{ECO:0000250|UniProtKB:O75116}.
MOD_RES 1362 1362 Phosphoserine.
{ECO:0000250|UniProtKB:O75116}.
MOD_RES 1374 1374 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1149 1149 P -> PVHITQSHTMESMSFTYQRSSTSLSIATKPSSSHTL
LDFDSEEDSLPYLPSSSEPIST (in isoform 2).
{ECO:0000303|PubMed:17606625}.
/FTId=VSP_041818.
VAR_SEQ 1388 1388 Missing (in isoform 2).
{ECO:0000303|PubMed:17606625}.
/FTId=VSP_041819.
SEQUENCE 1388 AA; 160586 MW; 7A4F331165038161 CRC64;
MSRPPPTGKM PGAPEAAPGD 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 GRNGVEEIKQ HPFFKNDQWN
WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYFRENL
LLSDSPPCRE NDAIQTRKSE ESQEIQKKLY ALEEHLSSEV QAKEELEQKC KSINTRLEKT
AKELEEEITL RKSVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL
EDLKKRNQSS QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKTGKA
LLAKVELEKR QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKT TKARLADKNK
IYESIEEAKS EAMKEMEKKL LEERSLKQKV ENLLLEAEKR CSILDCDLKQ SQQKLNELLK
QKDVLNEDVR NLTLKIEQET QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN
LEKQNTELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK
KQDLQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE
LTEKDTTIAS LEETNRTLTS DVANLANEKE ELNNKLKDSQ EQLSKLKDEE MSAAAIKAQF
EKQLLNERTL 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 LECRRCHIKC HKDHMDKKEE IIAPCKVYYD
ISSAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR
QLAPNKPS


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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
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
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
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
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
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
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
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
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
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
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
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
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
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
G8446 Rock-2 (Rho Associated Coiled Coil Containing Protein Kinase 2), Pig, ELISA Kit 96T
E-EL-P1911 Porcine Rock-2 (Rho Associated Coiled Coil Containing Protein Kinase 2) ELISA Kit 96T
E0308BO Canine Rho-associated coiled-coil containing protein kinase 2,Rock-2 ELISA Kit 48T
UT-E04648 Human Rho-Associated Coiled-coil Containing Protein Kinase 2 (Rock-2) ELISA Kit 96T
UB-E04648 Human Rho-associated coiled-coil containing protein kinase 2(Rock-2)ELISA Kit 96T


 

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