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Regulatory-associated protein of mTOR (Raptor) (p150 target of rapamycin (TOR)-scaffold protein)

 RPTOR_MOUSE             Reviewed;        1335 AA.
Q8K4Q0; Q8C9W9; Q8CBY4; Q8CDY8; Q9D4H3;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
22-NOV-2017, entry version 141.
RecName: Full=Regulatory-associated protein of mTOR;
Short=Raptor;
AltName: Full=p150 target of rapamycin (TOR)-scaffold protein;
Name=Rptor; Synonyms=Raptor;
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).
PubMed=12150926; DOI=10.1016/S0092-8674(02)00833-4;
Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S.,
Tokunaga C., Avruch J., Yonezawa K.;
"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR
action.";
Cell 110:177-189(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
STRAIN=C57BL/6J; TISSUE=Diencephalon, Head, Testis, and Thymus;
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).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[4]
PHOSPHORYLATION AT SER-722 AND SER-792, AND MUTAGENESIS OF SER-722 AND
SER-792.
PubMed=18439900; DOI=10.1016/j.molcel.2008.03.003;
Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A.,
Vasquez D.S., Turk B.E., Shaw R.J.;
"AMPK phosphorylation of raptor mediates a metabolic checkpoint.";
Mol. Cell 30:214-226(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-863, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6]
PHOSPHORYLATION AT SER-859 AND SER-863 BY MTOR.
PubMed=19346248; DOI=10.1074/jbc.C109.002907;
Wang L., Lawrence J.C. Jr., Sturgill T.W., Harris T.E.;
"Mammalian target of rapamycin complex 1 (mTORC1) activity is
associated with phosphorylation of raptor by mTOR.";
J. Biol. Chem. 284:14693-14697(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863; THR-865
AND SER-877, 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).
[8]
INTERACTION WITH MTOR.
PubMed=20801936; DOI=10.1101/gad.1956410;
Takai H., Xie Y., de Lange T., Pavletich N.P.;
"Tel2 structure and function in the Hsp90-dependent maturation of mTOR
and ATR complexes.";
Genes Dev. 24:2019-2030(2010).
-!- FUNCTION: Involved in the control of the mammalian target of
rapamycin complex 1 (mTORC1) activity which regulates cell growth
and survival, and autophagy in response to nutrient and hormonal
signals; functions as a scaffold for recruiting mTORC1 substrates.
mTORC1 is activated in response to growth factors or amino acids.
Growth factor-stimulated mTORC1 activation involves a AKT1-
mediated phosphorylation of TSC1-TSC2, which leads to the
activation of the RHEB GTPase that potently activates the protein
kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires
its relocalization to the lysosomes mediated by the Ragulator
complex and the Rag GTPases. Activated mTORC1 up-regulates protein
synthesis by phosphorylating key regulators of mRNA translation
and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and
releases it from inhibiting the elongation initiation factor 4E
(eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389',
which then promotes protein synthesis by phosphorylating PDCD4 and
targeting it for degradation. Involved in ciliogenesis.
{ECO:0000250|UniProtKB:Q8N122}.
-!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
(mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and
DEPTOR (PubMed:20801936). mTORC1 binds to and is inhibited by
FKBP12-rapamycin. Binds directly to 4EBP1 and RPS6KB1
independently of its association with MTOR. Binds preferentially
to poorly or non-phosphorylated forms of EIF4EBP1, and this
binding is critical to the ability of MTOR to catalyze
phosphorylation. Forms a complex with MTOR under both leucine-rich
and -poor conditions. Interacts with ULK1 in a nutrient-dependent
manner; the interaction is reduced during starvation. Interacts
(when phosphorylated by AMPK) with 14-3-3 protein, leading to
inhibition of its activity. Interacts with SPAG5; SPAG5 competes
with MTOR for RPTOR-binding, resulting in decreased mTORC1
formation. Interacts with WAC; WAC positively regulates MTOR
activity by promoting the assembly of the TTT complex composed of
TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and
RUVBL2 into the TTT-RUVBL complex which leads to the dimerization
of the mTORC1 complex and its subsequent activation. Interacts
with G3BP1. The complex formed with G3BP1 AND SPAG5 is increased
by oxidative stress. Interacts with HTR6. Interacts with PIH1D1.
Interacts with LARP1. Interacts with BRAT1.
{ECO:0000250|UniProtKB:Q8N122, ECO:0000269|PubMed:20801936}.
-!- INTERACTION:
Q9JLN9:Mtor; NbExp=9; IntAct=EBI-4567273, EBI-1571628;
Q00899:Yy1; NbExp=3; IntAct=EBI-4567273, EBI-6921536;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lysosome
{ECO:0000250}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q8N122}.
Note=Targeting to lysosomes depends on amino acid availability. In
arsenite-stressed cells, accumulates in stress granules when
associated with SPAG5 and association with lysosomes is
drastically decreased. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8K4Q0-1; Sequence=Displayed;
Name=2;
IsoId=Q8K4Q0-2; Sequence=VSP_010175, VSP_010181, VSP_010182;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8K4Q0-3; Sequence=VSP_010177, VSP_010179, VSP_010180;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8K4Q0-4; Sequence=VSP_010176, VSP_010183, VSP_010184;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q8K4Q0-5; Sequence=VSP_010178;
Note=No experimental confirmation available.;
-!- PTM: Insulin-stimulated phosphorylation at Ser-863 by MTOR and
MAPK8 up-regulates mTORC1 activity. Osmotic stress also induces
phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863
phosphorylation is required for phosphorylation at Ser-855 and
Ser-859 (By similarity). In response to nutrient limitation,
phosphorylated by AMPK; phosphorylation promotes interaction with
14-3-3 proteins, leading to negative regulation of the mTORC1
complex. In response to growth factors, phosphorylated at Ser-719,
Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.
{ECO:0000250|UniProtKB:Q8N122, ECO:0000269|PubMed:18439900,
ECO:0000269|PubMed:19346248}.
-!- SIMILARITY: Belongs to the WD repeat RAPTOR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AK029341; Type=Frameshift; Positions=22; Evidence={ECO:0000305};
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EMBL; AB082952; BAC06491.1; -; mRNA.
EMBL; AK016530; BAB30288.1; -; mRNA.
EMBL; AK029341; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK034306; BAC28669.1; -; mRNA.
EMBL; AK040288; BAC30561.1; -; mRNA.
CCDS; CCDS25720.1; -. [Q8K4Q0-1]
UniGene; Mm.209933; -.
UniGene; Mm.442144; -.
UniGene; Mm.450470; -.
UniGene; Mm.462932; -.
ProteinModelPortal; Q8K4Q0; -.
DIP; DIP-46324N; -.
IntAct; Q8K4Q0; 4.
MINT; MINT-4607805; -.
STRING; 10090.ENSMUSP00000026671; -.
iPTMnet; Q8K4Q0; -.
PhosphoSitePlus; Q8K4Q0; -.
EPD; Q8K4Q0; -.
PaxDb; Q8K4Q0; -.
PeptideAtlas; Q8K4Q0; -.
PRIDE; Q8K4Q0; -.
UCSC; uc007mqw.1; mouse. [Q8K4Q0-5]
UCSC; uc007mra.1; mouse. [Q8K4Q0-1]
MGI; MGI:1921620; Rptor.
eggNOG; KOG1517; Eukaryota.
eggNOG; ENOG410XQKJ; LUCA.
HOGENOM; HOG000184479; -.
HOVERGEN; HBG059496; -.
InParanoid; Q8K4Q0; -.
PhylomeDB; Q8K4Q0; -.
ChiTaRS; Rptor; mouse.
PRO; PR:Q8K4Q0; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_4932417H02RIK; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0031931; C:TORC1 complex; ISS:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
GO; GO:0030674; F:protein binding, bridging; ISO:MGI.
GO; GO:0032403; F:protein complex binding; ISO:MGI.
GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI.
GO; GO:0001030; F:RNA polymerase III type 1 promoter DNA binding; ISO:MGI.
GO; GO:0001031; F:RNA polymerase III type 2 promoter DNA binding; ISO:MGI.
GO; GO:0001032; F:RNA polymerase III type 3 promoter DNA binding; ISO:MGI.
GO; GO:0001156; F:TFIIIC-class transcription factor binding; ISO:MGI.
GO; GO:0016049; P:cell growth; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0071233; P:cellular response to leucine; ISO:MGI.
GO; GO:0031669; P:cellular response to nutrient levels; ISO:MGI.
GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:CACAO.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; ISO:MGI.
GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
GO; GO:0008361; P:regulation of cell size; ISO:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:CACAO.
GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
GO; GO:0038202; P:TORC1 signaling; ISO:MGI.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000357; HEAT.
InterPro; IPR004083; Raptor.
InterPro; IPR029347; Raptor_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR12848; PTHR12848; 1.
Pfam; PF02985; HEAT; 1.
Pfam; PF14538; Raptor_N; 1.
Pfam; PF00400; WD40; 1.
SMART; SM01302; Raptor_N; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Lysosome;
Phosphoprotein; Reference proteome; Repeat; WD repeat.
CHAIN 1 1335 Regulatory-associated protein of mTOR.
/FTId=PRO_0000051201.
REPEAT 1020 1061 WD 1.
REPEAT 1065 1106 WD 2.
REPEAT 1121 1160 WD 3.
REPEAT 1164 1203 WD 4.
REPEAT 1209 1249 WD 5.
REPEAT 1251 1291 WD 6.
REPEAT 1299 1335 WD 7.
MOD_RES 696 696 Phosphoserine; by MAPK8.
{ECO:0000250|UniProtKB:Q8N122}.
MOD_RES 706 706 Phosphothreonine; by MAPK8.
{ECO:0000250|UniProtKB:Q8N122}.
MOD_RES 719 719 Phosphoserine; by RPS6KA1.
{ECO:0000250|UniProtKB:Q8N122}.
MOD_RES 721 721 Phosphoserine; by RPS6KA1.
{ECO:0000250|UniProtKB:Q8N122}.
MOD_RES 722 722 Phosphoserine; by AMPK and RPS6KA1.
{ECO:0000269|PubMed:18439900}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N122}.
MOD_RES 792 792 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:18439900}.
MOD_RES 855 855 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N122}.
MOD_RES 859 859 Phosphoserine; by MTOR.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:19346248}.
MOD_RES 863 863 Phosphoserine; by MAPK8 and MTOR.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:19346248}.
MOD_RES 865 865 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 877 877 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 954 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010176.
VAR_SEQ 1 421 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010177.
VAR_SEQ 1 185 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010175.
VAR_SEQ 298 1335 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010178.
VAR_SEQ 701 728 EGGSLTPVRDSPCTPRLRSVSSYGNIRA -> GTGVAGSLG
PPSGPSPGQSVAWVQPGQV (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010179.
VAR_SEQ 729 1335 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010180.
VAR_SEQ 841 843 ATV -> VCI (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010181.
VAR_SEQ 844 1335 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010182.
VAR_SEQ 1202 1202 C -> W (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010183.
VAR_SEQ 1203 1335 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_010184.
MUTAGEN 722 722 S->A: Abolishes AMPK-mediated
phosphorylation; when associated with A-
792. {ECO:0000269|PubMed:18439900}.
MUTAGEN 792 792 S->A: Abolishes AMPK-mediated
phosphorylation; when associated with A-
722. {ECO:0000269|PubMed:18439900}.
CONFLICT 630 630 S -> F (in Ref. 2; AK029341/BAB30288).
{ECO:0000305}.
CONFLICT 970 970 A -> P (in Ref. 2; BAC30561).
{ECO:0000305}.
SEQUENCE 1335 AA; 149471 MW; 26702199FF7C8136 CRC64;
MESEMLQSPL MGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV
ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK
QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY
DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC
IQLAACEAHE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY
NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL
TMGVENRSPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL
QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA
VIVNSYTTGQ EACLQGNLIA ICLEQLSDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LINDGSPMVR
KELVVALSHL VVQYESNFCT VALQFMEEEK NYPLPSPAAT EGGSLTPVRD SPCTPRLRSV
SSYGNIRAVT TARNLNKSLQ NLSLTEESGS SVAFSPGNLS TSSSASSTLG SPENEEYILS
FETIDKMRRV SSYSALNSLI GVSFNSVYTQ IWRVLLHLAA DPYPDVSDLA MKVLNSIAYK
ATVNARPQRI LDTSSLTQSA PASPTNKGMH MHQVGGSPPA SSTSSCSLTN DVAKQTVSRD
LPSSRPGTAG PTGAQYTPHS HQFPRTRKMF DKGPDQTTDD ADDAAGHKSF ICASMQTGFC
DWSARYFAQA VMKIPEEHDL ESQIRKEREW RFLRNTRVRK QAQQVIQKGI TRLDDQIFLN
RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD
CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS
SGDVRIVRIW DTDRETKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS
ECRVMTYREH TAWVVKAYLQ KHPEGHIVSV SVNGDVRFFD PRMPESVNVM QIVKGLTALD
IHPQANLIAC GSMNQFTAIY NGNGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS
NDYYISVYSV EKRVR


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EIAAB25746 FK506-binding protein 12-rapamycin complex-associated protein 1,FKBP12-rapamycin complex-associated protein,Frap,Frap1,Mammalian target of rapamycin,Mechanistic target of rapamycin,Mouse,mTOR,Mtor,Mus
EIAAB25745 FK506-binding protein 12-rapamycin complex-associated protein 1,FKBP12-rapamycin complex-associated protein,Frap1,Mammalian target of rapamycin,Mechanistic target of rapamycin,mTOR,Mtor,Raft1,Rapamyci
18-785-210287 mTOR (Phospho-Ser2448) - FK506-binding protein 12-rapamycin complex-associated protein 1; Rapamycin target protein; RAPT1; Mammalian target of rapamycin; mTOR Polyclonal 0.1 mg
18-785-210287 mTOR (Phospho-Ser2448) - FK506-binding protein 12-rapamycin complex-associated protein 1; Rapamycin target protein; RAPT1; Mammalian target of rapamycin; mTOR Polyclonal 0.05 mg
18-661-15231 FKBP12-rapamycin complex-associated protein - FK506-binding protein 12-rapamycin complex-associated protein 1; Rapamycin target protein; RAPT1; Mammalian target of rapamycin; mTOR Polyclonal 0.1 mg
EIAAB25744 FK506-binding protein 12-rapamycin complex-associated protein 1,FKBP12-rapamycin complex-associated protein,FRAP,FRAP1,FRAP2,Homo sapiens,Human,Mammalian target of rapamycin,Mechanistic target of rapa
mTOR-101AP PC-mTOR (WB control) Mammalian Target of Rapamycin (mTOR) Immunogen: peptide Host: Rabbit 100-150ul
mTOR-101AP Mammalian Target of Rapamycin (mTOR) WB control: PC-mTOR Host: Rabbit Affinity purifed 100-150ul
mTOR-101AP Mammalian Target of Rapamycin (mTOR) Antigenic peptide: P-mTOR Host: Rabbit Affinity purifed 100ul
bs-1992P Peptides: mTOR(Mammalian target of rapamycin) Protein Length:12-25 amino acids. 200ug lyophilized
mTOR-101AP mTOR-FITC (FITC-conjugates) Mammalian Target of Rapamycin (mTOR) Immunogen: peptide Host: Rabbit 200ul
mTOR-101AP mTOR-Biotin (Biotin Conjugates) Mammalian Target of Rapamycin (mTOR) Immunogen: peptide Host: Rabbit 200ul
mTOR-101AP Mammalian Target of Rapamycin (mTOR) FITC-conjugates: mTOR-FITC Host: Rabbit Affinity purifed 200ul
mTOR-101AP Mammalian Target of Rapamycin (mTOR) Biotin Conjugates: mTOR-Biotin Host: Rabbit Affinity purifed 200ul
mTOR-101AP P-mTOR (Antigenic peptide) Mammalian Target of Rapamycin (mTOR) Immunogen: peptide Host: Rabbit 100ul
P-mTOR Mammalian Target of Rapamycin (mTOR) , Antigen blocking peptide 100ul
mTOR-101AP Mammalian Target of Rapamycin (mTOR) , Host species: rabbit, polyclonal antibody 200ul
mTOR-101AP Polyclonal Antibody Mammalian Target of Rapamycin (mTOR) Immunogen: peptide Host: Rabbit 200ul


 

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