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Leucine-rich repeat kinase 2

 F1LNJ1_RAT              Unreviewed;      2526 AA.
F1LNJ1;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 3.
20-JUN-2018, entry version 70.
SubName: Full=Leucine-rich repeat kinase 2 {ECO:0000313|Ensembl:ENSRNOP00000005438};
Name=Lrrk2 {ECO:0000313|Ensembl:ENSRNOP00000005438,
ECO:0000313|RGD:1561168};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000005438, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000005438, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000005438,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|Ensembl:ENSRNOP00000005438}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000005438};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
[3] {ECO:0000213|PubMed:22673903}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
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EMBL; AC108595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_006242252.1; XM_006242190.3.
UniGene; Rn.213971; -.
IntAct; F1LNJ1; 2.
STRING; 10116.ENSRNOP00000005438; -.
iPTMnet; F1LNJ1; -.
PhosphoSitePlus; F1LNJ1; -.
PaxDb; F1LNJ1; -.
PRIDE; F1LNJ1; -.
Ensembl; ENSRNOT00000005438; ENSRNOP00000005438; ENSRNOG00000004048.
GeneID; 300160; -.
CTD; 120892; -.
RGD; 1561168; Lrrk2.
eggNOG; KOG0192; Eukaryota.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG1100; LUCA.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00910000144054; -.
InParanoid; F1LNJ1; -.
OMA; FKIRDQP; -.
OrthoDB; EOG091G003N; -.
TreeFam; TF313679; -.
Reactome; R-RNO-8857538; PTK6 promotes HIF1A stabilization.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000004048; -.
GO; GO:0044753; C:amphisome; IEA:Ensembl.
GO; GO:0044754; C:autolysosome; IEA:Ensembl.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0099400; C:caveola neck; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005798; C:Golgi-associated vesicle; IEA:Ensembl.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IBA:GO_Central.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0097487; C:multivesicular body, internal vesicle; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:1990909; C:Wnt signalosome; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:1904713; F:beta-catenin destruction complex binding; IEA:Ensembl.
GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:Ensembl.
GO; GO:0034211; F:GTP-dependent protein kinase activity; IEA:Ensembl.
GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; IEA:Ensembl.
GO; GO:0036479; F:peroxidase inhibitor activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0051018; F:protein kinase A binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0017048; F:Rho GTPase binding; IBA:GO_Central.
GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
GO; GO:0000186; P:activation of MAPKK activity; IEA:Ensembl.
GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
GO; GO:0034613; P:cellular protein localization; ISS:ParkinsonsUK-UCL.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
GO; GO:0006897; P:endocytosis; IEA:Ensembl.
GO; GO:0060079; P:excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
GO; GO:0046039; P:GTP metabolic process; IEA:Ensembl.
GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; ISS:ParkinsonsUK-UCL.
GO; GO:0035641; P:locomotory exploration behavior; ISS:ParkinsonsUK-UCL.
GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IBA:GO_Central.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ParkinsonsUK-UCL.
GO; GO:0010955; P:negative regulation of protein processing; IEA:Ensembl.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IEA:Ensembl.
GO; GO:1903125; P:negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
GO; GO:0070997; P:neuron death; IEA:Ensembl.
GO; GO:0140058; P:neuron projection arborization; IMP:RGD.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; IEA:Ensembl.
GO; GO:1903980; P:positive regulation of microglial cell activation; IMP:RGD.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
GO; GO:0043068; P:positive regulation of programmed cell death; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:1902499; P:positive regulation of protein autoubiquitination; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:RGD.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:RGD.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; IEA:Ensembl.
GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IEA:Ensembl.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:ParkinsonsUK-UCL.
GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0035564; P:regulation of kidney size; IEA:Ensembl.
GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
GO; GO:0035751; P:regulation of lysosomal lumen pH; IEA:Ensembl.
GO; GO:0051900; P:regulation of mitochondrial depolarization; IEA:Ensembl.
GO; GO:1902692; P:regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0014041; P:regulation of neuron maturation; IEA:Ensembl.
GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:ParkinsonsUK-UCL.
GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IBA:GO_Central.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:ParkinsonsUK-UCL.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:1902803; P:regulation of synaptic vesicle transport; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
GO; GO:0021756; P:striatum development; IEP:RGD.
GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
GO; GO:1904887; P:Wnt signalosome assembly; IEA:Ensembl.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR032171; COR.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR020859; ROC_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF16095; COR; 1.
Pfam; PF12799; LRR_4; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 6.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48371; SSF48371; 3.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF56112; SSF56112; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51450; LRR; 11.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS51424; ROC; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Leucine-rich repeat {ECO:0000256|SAAS:SAAS00537711};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Repeat {ECO:0000256|SAAS:SAAS00537628}.
DOMAIN 1327 1510 Roc. {ECO:0000259|PROSITE:PS51424}.
DOMAIN 1878 2145 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
SEQUENCE 2526 AA; 284831 MW; DB5CA86E1E96E716 CRC64;
MASGACQGCD EEEEEEALKK LIVRLNNVQE GKQIETLLQL LEDILVFTYS DRASKLFEGK
NVHVPLLIVL DSYMRVASVQ QVGWSLLCKL IEVCPGTLQS LIGPQDIGND WEVLGIHRLI
LKMLTVHHAN VNLSIVGLKA LDLLLDSGKI TLLILDEECD VFLLIFDAMH RYSANEEVQK
LACKALHVLF ERVSEEQLTE FVENKDYMTL LSTFRSFKRD EEIVHHVLCC LHSLAVTCSN
VEVLMSGNVR CYNIVVEAMK TFPTSENIQE VSCSLLHKLT LGNFFNILVL NEVHVFVVKA
VQRYPENVAL QISALSCLAL LTETIFLNQD LEERSETQEN SDEDSEKPFW LEPCYKALMR
HRKNKHVQEA ACWALNNLLM YQSSLHEKIG DEDGQFPAHR EVMLSMLMHS SSKDVFQAAA
HALSTLLEQN VNFRKILLAK GVYLNVLELM QRHAQVPEVA ESGCKMLSHL FEGSNPSLDT
VAAVIPKILT VMRTHGTSLS VQLEALRALL HFVVPGVSED SRDDSRCQPN VLRTQCFRTD
IHKLVLAALN RFIGNPGIQK CGLKVISSFA HLPDALEMLS LHGAVDSVLH TLQMYPDDQE
IQCLGLHLMG CLMTKKNFCI GTGHLLAKIL ASTLQRFKDV AEVQTTGLQT VLSMLDLSVS
FSKLLVHYSF DVVMFHQMSS GVLEQKDEQF LNLCCKCFAK VAVDDELKSK MLERACDQNN
SIMVECLLLL GADANQAKGA TSLIYQVCEK ESSPKLVELL LNSGCREQDV RKALTVSIQK
GDNQVISLLL RRLALDLANN SICLGGFCIG KLDPSWLGPL FPDKSSNLRK QTNAGSVLAR
KVLRYQMRNT LQEGVASGSE GNFSEDALAK FGEWTFIPDS SMDSVFGQSD DLDSEGSESS
FLVKKKSNSV SVGEVYRDLA LQRCSPNAQR HSSSLGPVFD HEDLLRRKRK ILSSDESLRS
SRLQSHTRQS DSSSSLASER EHITSLDLSA NELKDIDALG QKCCLSSHLE HLTKLELHQN
SLTSFPQQLC ETLKCLTHLD LHSNKFATFP SFMLKMPSVI HLDASRNDIG PTVVLDPVVK
CPSLKQFNLS YNQLSSIPEN LDQVVEKLEQ LLLEGNKISG ICSPLSLKEL KILNLSKNHI
PSLPEDFLEA CPKVESFSAR MNFLAAMPAL PSSITSLKLS QNSFTCIPEA IFSLPHLRSL
DMSHNNIEHL PGPAHWKSLN LRELIFSKNQ ISTLDLSENP HIWSRVEKLH LSHNKLKEIP
PEIGRLENLT SLDVSYNLEL RSFPNEMGKL SKIWDLPLDG LHLNFDFKHI GCKAKDIIRF
LQQRLKKAVP YNRMKLMIVG NTGSGKTTLL QQLMKMKKSE LGMQGATVGI DVRDWPIQIR
GKRKKDLVLN VWDFAGREEF YSTHPHFMTQ RALYLAVYDL SKGQAEVDAM KPWLFNIKAR
ASSSPVILVG THLDVSDEKQ RKACIGKITK ELLNKRGFPT IRDYHFVNAT EESDALAKLR
KTIINESLNF KIRDQPVVGQ LIPDCYVELE KIILSERKAV PTEFPVINRK HLLQLVKEHQ
LQLDENELPH AVHFLNESGV LLHFQDPALQ LSDLYFVEPK WLCKVMAQIL TVKVDGCLKH
PKGIISRRDV EKFLSKKKRF PKNYMAQYFK LLEKFQIALP IGEEYLLVPS SLSDHRPVIE
LPHCENSEII IRLYEMPYFP MGFWSRLINR LLEISPFMLS GRERALRPNR MYWRQGIYLN
WSPEAYCLVG SEVLDSRPES FLKITVPSCR KGCILLGRVV DHIDSLMEEW FPGLLEIDIC
GEGETLLKKW ALYSFNDGEE HQKILLDELM KKAEEGDLLI NPDQPRLTIP ISQIAPDLIL
ADLPRNIMLN NDELEFEEAP EFLLGDGSFG SVYRAAYEGE EVAVKIFNKH TSLRLLRQEL
VVLCHLHHPS LISLLAAGIR PRMLVMELAS KGSLDRLLQQ DKASLTRTLQ HRIALHVADG
LRYLHSAMII YRDLKPHNVL LFTLYPNAAI IAKIADYGIA QYCCRMGIKT SEGTPGFRAP
EVARGNVIYN QQADVYSFGL LLHDIWTTGN RIMEGLRFPN EFDELAIQGK LPDPVKEYGC
APWPMVEKLI TKCLKENPQE RPTSAQVFDI LNSAELICLM RHIFIPKDIT VECIAATNLN
SKRATLWLGC GNTEKGQLSL LDLNTERYSY EEVTDSRILC LALVHLAAEK ESWVVCGTQS
GALLVINAED ETRRHTLDKM TDSVTCLYCN SFAKQSKQSH FLLVGTADGN LMIFEDKTIK
CKGAAPLKTL HIGDVSTPLM CLSESMNSSE RHITWGGCGT KIFSFSNDFT IQKLIETRTN
QLFSYSAFSD SNIIAVAVDT ALYIAKKNSP VVEVWDKKTE KLCELIDCVH FLKEVMVKIN
KDSKHKLSYS GRVKALCLQK NTALWIGTGG GHILLLDLST RRVIRTIHNF CDSVRAMATA
QLGSLKNVML VLGYKRKSTE GTQEQKEIQS CLSIWDLNLP HEVQNLEKHI EVRTELADKM
RKTSVE


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EIAAB43980 Homo sapiens,Human,KIAA0644,Leucine-rich repeat-containing protein KIAA0644,TLR4 interactor with leucine rich repeats,TRIL
RCN3_HUMAN Human ELISA Kit FOR Leucine-rich repeat serine per threonine-protein kinase 1 96T
LRRK2-1030H Protein Recombinant Human Leucine-Rich Repeat Kinase 2, GST-tagged 5
TIAM2_MOUSE Mouse ELISA Kit FOR Leucine-rich repeat and guanylate kinase domain-containing protein 96T
DB136_HUMAN Mouse ELISA Kit FOR Leucine-rich repeat and guanylate kinase domain-containing protein 96T
CSB-EL013180HU Human Leucine-rich repeat serine_threonine-protein kinase 1(LRRK1) ELISA kit 96T
E0552r Human ELISA Kit FOR Leucine-rich repeat serine per threonine-protein kinase 1 96T
CSB-EL013181HU Human Leucine-rich repeat serine_threonine-protein kinase 2(LRRK2) ELISA kit 96T
SEH716Hu ELISA Kit for Leucine Rich Repeat Kinase 2 (LRRK2) Homo sapiens (Human) 96T
E0190m Mouse ELISA Kit FOR Leucine-rich repeat and guanylate kinase domain-containing protein 96T
LRRK2-1030H Protein: Recombinant Human Leucine-Rich Repeat Kinase 2, GST-tagged 5
CSB-EL013181MO Mouse Leucine-rich repeat serine_threonine-protein kinase 2(LRRK2) ELISA kit 96T
CSB-EL013180MO Mouse Leucine-rich repeat serine_threonine-protein kinase 1(LRRK1) ELISA kit 96T


 

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