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ELISA Kit for Bovine Rho-associated protein kinase 2

SKU : BHE13809981

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1852b
Alternative Names	Rho-associated ; coiled-coil-containing protein kinase 2 ; Rho-associated ; coiled-coil-containing protein kinase II ; ROCK-II ; 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.
Specificity	Natural and recombinant Bovine 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.
Entryname	ROCK2_BOVIN
Platform	PF02185
Protein Name	Rho-associated protein kinase 2
Sequence	50: MSRPPPTGKM ; PGAPEAVSGD ; GAGASRQRKL ; EALIRDPRSP ; INVESLLDGL ; 100: NPLVLDLDFP ; ALRKNKNIDN ; FLNRYEKIVK ; KIRGLQMKAE ; DYDVVKVIGR ; 150: GAFGEVQLVR ; HKASQKVYAM ; KLLSKFEMIK ; RSDSAFFWEE ; RDIMAFANSP ; 200: WVVQLFCAFQ ; DDKYLYMVME ; YMPGGDLVNL ; MSNYDVPEKW ; AKFYTAEVVL ; 250: ALDAIHSMGL ; IHRDVKPDNM ; LLDKHGHLKL ; ADFGTCMKMD ; ETGMVHCDTA ; 300: VGTPDYISPE ; VLKSQGGDGY ; YGRECDWWSV ; GVFLFEMLVG ; DTPFYADSLV ; 350: GTYSKIMDHK ; NSLCFPEDAE ; ISKHAKNLIC ; AFLTDREVRL ; GRNGVEEIKQ ; 400: HPFFKNDQWN ; WDNIRETAAP ; VVPELSSDID ; SSNFDDIEDD ; KGDVETFPIP ; 450: KAFVGNQLPF ; IGFTYYRENL ; LLSDSPSCKE ; NDSIQSRKNE ; ESQEIQKKLY ; 500: TLEEHLSTEI ; QAKEELEQKC ; KSVNTRLEKV ; AKELEEEITL ; RKNVESTLRQ ; 550: LEREKALLQH ; KNAEYQRKAD ; HEADKKRNLE ; NDVNSLKDQL ; EDLKKRNQNS ; 600: QISTEKVNQL ; QRQLDETNAL ; LRTESDTAAR ; LRKTQAESSK ; QIQQLESNNR ; 650: DLQDKNCLLE ; TAKLKLEKEF ; INLQSVLESE ; RRDRTHGSEI ; INDLQGRISG ; 700: LEEDVKNGKI ; LLAKVELEKR ; QLQERFTDLE ; KEKNNMEIDM ; TYQLKVIQQS ; 750: LEQEETEHKA ; TKARLADKNK ; IYESIEEAKS ; EAMKEMEKKL ; SEERTLKQKV ; 800: ENLLLEAEKR ; CSILDCDLKQ ; SQQKINELLK ; QKDVLNEDVR ; NLTLKIEQET ; 850: QKRCLTQNDL ; KMQTQQVNTL ; KMSEKQLKQE ; NNHLLEMKMS ; LEKQNAELRK ; 900: ERQDADGQMK ; ELQDQLEAEQ ; YFSTLYKTQV ; RELKEECEEK ; TKLCKELQQK ; 950: KQELQDERDS ; LAAQLEITLT ; KADSEQLARS ; IAEEQYSDLE ; KEKIMKELEI ; 1000: KEMMARHKQE ; LTEKDATIAS ; LEETNRTLTS ; DVANLANEKE ; ELNNKLKEAQ ; 1050: EQLSRLKDEE ; ISAAAIKAQF ; EKQLLTERTL ; KTQAVNKLAE ; IMNRKEPVKR ; 1100: GNDTDVRRKE ; KENRKLHMEL ; KSEREKLTQQ ; MIKYQKELNE ; MQAQIAEESQ ; 1150: IRIELQMTLD ; SKDSDIEQLR ; SQLQALHIGL ; DSSSIGSGPG ; DTEADDGFPE ; 1200: SRLEGWLSLP ; VRNNTKKFGW ; VKKYVIVSSK ; KILFYDSEQD ; KEQSNPYMVL ; 1250: DIDKLFHVRP ; VTQTDVYRAD ; AKEIPRIFQI ; LYANEGESKK ; EQEFPVEPVG ; 1300: EKSNYICHKG ; HEFIPTLYHF ; PTNCEACMKP ; LWHMFKPPPA ; LECRRCHIKC ; 1350: HKDHMDKKEE ; IIAPCKVYYD ; ISSAKNLLLL ; ANSTEEQQKW ; VSRLVKKIPK ; 1388: KPPAPDPFAR ; SSPRTSMKIQ ; QNQSIRRPSR ; QLAPNKPS
Sequence Length	1388
String	Q28021
Sub Unit	Homodimer (By similarity). Interacts with RHOA (activated by GTP), CHORDC1, IRS1, RHOB, RHOC, PPP1R12A, SORL1, EP300 and BRCA2 (By similarity). Interacts with NPM1 and this interaction enhances its activity.

Uniprot	Q28021
Gene Name	ROCK2
Immunogen Species	Bos Taurus (Cattle)
Kegg	bta:282041
Unigene	Bt.120

Reference	1. "Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho." Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K. EMBO J.15:2208-2216(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: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 10-18; 30-44; 58-64; 133-140; 248-252; 291-305; 327-348; 350-360; 366-384; 392-400; 506-511; 527-535; 590-604; 633-652; 670-681; 829-842; 861-872; 913-921; 947-950; 979-988; 1066-1070; 1087-1091; 1114-1120; 1131-1141; 1145-1151; 1158-1166; 1182-1191; 1198-1218 AND 1318-1325;FUNCTION;INTERACTION WITH RHOA;PHOSPHORYLATION;TISSUE SPECIFICITY;SUBCELLULAR LOCATION 2. "Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase)." Amano M., Ito M., Kimura K., Fukata Y., Chihara K., Nakano T., Matsuura Y., Kaibuchi K. J. Biol. Chem.271:20246-20249(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 3. "Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis." Goto H., Kosako H., Tanabe K., Yanagida M., Sakurai M., Amano M., Kaibuchi K., Inagaki M. J. Biol. Chem.273:11728-11736(1998) [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 4. "Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association." Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., Tsukita S., Tsukita S. J. Cell Biol.140:647-657(1998) [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 5. "Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility." Fukata Y., Oshiro N., Kinoshita N., Kawano Y., Matsuoka Y., Bennett V., Matsuura Y., Kaibuchi K. J. Cell Biol.145:347-361(1999) [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 6. "Identification of calponin as a novel substrate of Rho-kinase." Kaneko T., Amano M., Maeda A., Goto H., Takahashi K., Ito M., Kaibuchi K. Biochem. Biophys. Res. Commun.273:110-116(2000) [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 7. "Phosphorylation of collapsin response mediator protein-2 by Rho-kinase. Evidence for two separate signaling pathways for growth cone collapse." Arimura N., Inagaki N., Chihara K., Menager C., Nakamura N., Amano M., Iwamatsu A., Goshima Y., Kaibuchi K. J. Biol. Chem.275:23973-23980(2000) [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 8. "Parallel coiled-coil association of the RhoA-binding domain in Rho-kinase." Shimizu T., Ihara K., Maesaki R., Amano M., Kaibuchi K., Hakoshima T. J. Biol. Chem.278:46046-46051(2003) [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: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 979-1047 IN COMPLEX WITH RHOA;HOMODIMERIZATION

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