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ELISA Kit for Rat Rho-associated protein kinase 2

SKU : BHE13809871

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1852r
Alternative Names	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
Categories	Elisa
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.
Specificity	Natural and recombinant Rat Rho-associated protein kinase 2
Subcellular Location	Cytoplasm Cell membrane Peripheral membrane protein Nucleus Cytoplasm cytoskeleton centrosome Cytoplasmic, and associated with actin microfilaments and the plasma membrane.
Detection Range	1.56-100ng/mL
Entryname	ROCK2_RAT
Method Type	Sandwich
Platform	PF02185
Protein Name	Rho-associated protein kinase 2
Sensitivity	0.87ng/mL
Sequence	50: MSRPPPTGKM ; PGAPEAAAGD ; GAGAGRQRKL ; EALIRDPRSP ; INVESLLDGL ; 100: NSLVLDLDFP ; ALRKNKNIDN ; FLNRYEKIVK ; KIRGLQMKAE ; DYDVVKVIGR ; 150: GAFGEVQLVR ; HKASQKVYAM ; KLLSKFEMIK ; RSDSAFFWEE ; RDIMAFANSP ; 200: WVVQLFCAFQ ; DDRYLYMVME ; YMPGGDLVNL ; MSNYDVPEKW ; AKFYTAEVVL ; 250: ALDAIHSMGL ; IHRDVKPDNM ; LLDKHGHLKL ; ADFGTCMKMD ; ETGMVHCDTA ; 300: VGTPDYISPE ; VLKSQGGDGY ; YGRECDWWSV ; GVFLFEMLVG ; DTPFYADSLV ; 350: GTYSKIMDHK ; NSLCFPEDTE ; ISKHAKNLIC ; AFLTDREVRL ; GRNGVEEIKS ; 400: ASFFKNDQWN ; WDNIRETAAP ; VVPELSSDID ; SSNFDDIEDD ; KGDVETFPIP ; 450: KAFVGNQLPF ; IGFTYFRENL ; LLSDSPPCRE ; NDAIQTRKSE ; ESQEIQKKLY ; 500: ALEEHLSSEV ; QAKEELEQKC ; KSINTRLEKT ; AKELEEEITF ; RKNVESTLRQ ; 550: LEREKALLQH ; KNAEYQRKAD ; HEADKKRNLE ; NDVNSLKDQL ; EDLKKRNQSS ; 600: QISTEKVNQL ; QKQLDEANAL ; LRTESDTAAR ; LRKTQAESSK ; QIQQLESNNR ; 650: DLQDKNCLLE ; TAKLKLEKEF ; INLQSALESE ; RRDRTHGSEI ; INDLQGRISG ; 700: LEEDLKTGKT ; LLAKVELEKR ; QLQEKLTDLE ; KEKSNMEIDM ; TYQLKVIQQS ; 750: LEQEEAEHKT ; TKARLADKNK ; IYESIEEAKS ; EAMKEMEKKL ; LEERSLKQKV ; 800: ENLLLEAEKR ; CSILDCDLKQ ; SQQKLNELLK ; QKDVLNEDVR ; NLTLKIEQET ; 850: QKRCLMQNDL ; KMQTQQVNTL ; KMSEKQIKQE ; NNHLMEMKMN ; LEKQNAELRK ; 900: ERQDADGQMK ; ELQDQLEAEQ ; YFSTLYKTQV ; RELKEENEEK ; TKLCKELQQK ; 950: KQDLQDERDS ; LAAQLEITLT ; KADSEQLARS ; IAEEQYSDLE ; KEKIMKELEI ; 1000: KEMMARHKQE ; LTEKDATIAS ; LEETNRTLTS ; DVANLANEKE ; ELNNKLKDTQ ; 1050: EQLSKLKDEE ; ISAAAIKAQF ; EKQLLTERTL ; KTQAVNKLAE ; IMNRKEPVKR ; 1100: GSDTDVRRKE ; KENRKLHMEL ; KSEREKLTQQ ; MIKYQKELNE ; MQAQIAEESQ ; 1150: IRIELQMTLD ; SKDSDIEQLR ; SQLQALHIGM ; DSSSIGSGPG ; DAEPDDGFPE ; 1200: SRLEGWLSLP ; VRNNTKKFGW ; VKKYVIVSSK ; KILFYDSEQD ; KEQSNPYMVL ; 1250: DIDKLFHVRP ; VTQTDVYRAD ; AKEIPRIFQI ; LYANEGESKK ; EPEFPVEPVG ; 1300: EKSNYICHKG ; HEFIPTLYHF ; PTNCEACMKP ; LWHMFKPPPA ; LECSRCHIKC ; 1350: HKDHMDKKEE ; IIAPCKVYYD ; ISSAKNLLLL ; ANSTEEQQKW ; VSRLVKKIPK ; 1388: KPPAPDPFAR ; SSPRTSMKIQ ; QNQSIRRPSR ; QLAPNKPS
Sequence Length	1388
String	Q62868
Sub Unit	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.

Uniprot	Q62868
Gene Name	Rock2
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:25537
Unigene	Rn.88642

Reference	1. "A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes." Leung T., Manser E., Tan L., Lim L. J. Biol. Chem.270:29051-29054(1995) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];FUNCTION;AUTOPHOSPHORYLATION;INTERACTION WITH RHOA;SUBCELLULAR LOCATION tissue: Brain. 2. "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton." Leung T., Chen X.-Q., Manser E., Lim L. Mol. Cell. Biol.16:5313-5327(1996) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;AUTOPHOSPHORYLATION;INTERACTION WITH RHOA; RHOB AND RHOC;MUTAGENESIS OF LYS-121;TISSUE SPECIFICITY 3. "Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension." Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T., Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S. Nature389:990-994(1997) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;ROLE IN HYPERTENSION;INHIBITION BY Y-27632 4. "Active Rho kinase (ROK-alpha) associates with insulin receptor substrate-1 and inhibits insulin signaling in vascular smooth muscle cells." Begum N., Sandu O.A., Ito M., Lohmann S.M., Smolenski A. J. Biol. Chem.277:6214-6222(2002) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH IRS1 5. "Raf-1 regulates Rho signaling and cell migration." Ehrenreiter K., Piazzolla D., Velamoor V., Sobczak I., Small J.V., Takeda J., Leung T., Baccarini M. J. Cell Biol.168:955-964(2005) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH RAF1 6. "Direct cleavage of ROCK II by granzyme B induces target cell membrane blebbing in a caspase-independent manner." Sebbagh M., Hamelin J., Bertoglio J., Solary E., Breard J. J. Exp. Med.201:465-471(2005) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: CLEAVAGE BY GRANZYME B 7. "The hydrophobic motif of ROCK2 requires association with the N-terminal extension for kinase activity." Couzens A.L., Saridakis V., Scheid M.P. Biochem. J.419:141-148(2009) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DOMAIN;PHOSPHORYLATION AT THR-414;MUTAGENESIS OF ASP-48; LYS-121; THR-414 AND TRP-1170 8. "ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells." Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K. Circ. Res.104:531-540(2009) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH PPP1R12A;SUBCELLULAR LOCATION 9. "Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase." Tan I., Lai J., Yong J., Li S.F., Leung T. FEBS Lett.585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF MYL9/MLC2 AND PPP1R12A

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