Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Phosphatase and tensin homolog (Phosphatase and tensin homolog, isoform CRA_a) (Protein tyrosine phosphatase and tensin homolog/mutated in multiple advanced cancers protein) (Protein tyrosine phosphatase and tensin-like protein)

 O54857_RAT              Unreviewed;       403 AA.
O54857;
01-JUN-1998, integrated into UniProtKB/TrEMBL.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 139.
SubName: Full=Phosphatase and tensin homolog {ECO:0000313|Ensembl:ENSRNOP00000028143};
SubName: Full=Phosphatase and tensin homolog, isoform CRA_a {ECO:0000313|EMBL:EDM13141.1};
SubName: Full=Protein tyrosine phosphatase and tensin homolog/mutated in multiple advanced cancers protein {ECO:0000313|EMBL:AAB96620.1};
SubName: Full=Protein tyrosine phosphatase and tensin-like protein {ECO:0000313|EMBL:AAO31948.1};
Name=Pten {ECO:0000313|EMBL:AAO31948.1,
ECO:0000313|Ensembl:ENSRNOP00000028143, ECO:0000313|RGD:61995};
Synonyms=PTEN/MMAC1 {ECO:0000313|EMBL:AAB96620.1};
ORFNames=rCG_47874 {ECO:0000313|EMBL:EDM13141.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000313|EMBL:AAB96620.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAB96620.1};
TISSUE=Brain {ECO:0000313|EMBL:AAB96620.1};
Roz L., Finocchiaro G.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AAO31948.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:AAO31948.1};
PubMed=12461751; DOI=10.1002/gcc.10143;
Sjoling A., Samuelson E., Adamovic T., Behboudi A., Rohme D.,
Levan G.;
"Recurrent allelic imbalance at the rat Pten locus in DMBA-induced
fibrosarcomas.";
Genes Chromosomes Cancer 36:70-79(2003).
[3] {ECO:0000313|Ensembl:ENSRNOP00000028143, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028143,
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).
[4] {ECO:0000313|EMBL:EDM13141.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM13141.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[5] {ECO:0000313|EMBL:EDM13141.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM13141.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000213|PDB:2K20}
STRUCTURE BY NMR OF 393-403.
Feng W., Wu H., Chan L., Zhang M.;
"Solution structure of Par-3 PDZ3 in complex with PTEN peptide.";
Submitted (MAR-2008) to the PDB data bank.
[7] {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).
[8] {ECO:0000313|Ensembl:ENSRNOP00000028143}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028143};
Ensembl;
Submitted (FEB-2012) to UniProtKB.
-!- INTERACTION:
Q07266:Dbn1; NbExp=3; IntAct=EBI-8074312, EBI-918187;
P31016:Dlg4; NbExp=5; IntAct=EBI-8074312, EBI-375655;
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AABR07006753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07006754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF017185; AAB96620.1; -; mRNA.
EMBL; AF455569; AAO31948.1; -; mRNA.
EMBL; CH473953; EDM13141.1; -; Genomic_DNA.
RefSeq; NP_113794.1; NM_031606.1.
UniGene; Rn.22158; -.
PDB; 2K20; NMR; -; B=393-403.
PDBsum; 2K20; -.
SMR; O54857; -.
IntAct; O54857; 3.
MINT; MINT-4583512; -.
STRING; 10116.ENSRNOP00000028143; -.
iPTMnet; O54857; -.
PhosphoSitePlus; O54857; -.
Ensembl; ENSRNOT00000028143; ENSRNOP00000028143; ENSRNOG00000020723.
GeneID; 50557; -.
KEGG; rno:50557; -.
CTD; 5728; -.
RGD; 61995; Pten.
eggNOG; KOG2283; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000119113; -.
HOGENOM; HOG000008008; -.
HOVERGEN; HBG000239; -.
KO; K01110; -.
OMA; PFDEEQH; -.
OrthoDB; EOG091G09VG; -.
TreeFam; TF324513; -.
BRENDA; 3.1.3.67; 5301.
Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-RNO-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-RNO-202424; Downstream TCR signaling.
Reactome; R-RNO-5689880; Ub-specific processing proteases.
Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
Reactome; R-RNO-8948747; Regulation of PTEN localization.
Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000020723; -.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0010997; F:anaphase-promoting complex binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; IEA:Ensembl.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IDA:RGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IDA:RGD.
GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; IEA:Ensembl.
GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:Ensembl.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:RGD.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
GO; GO:1990782; F:protein tyrosine kinase binding; IDA:RGD.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:Ensembl.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; TAS:RGD.
GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
GO; GO:0030534; P:adult behavior; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
GO; GO:0071361; P:cellular response to ethanol; IDA:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:RGD.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IDA:RGD.
GO; GO:0044320; P:cellular response to leptin stimulus; IMP:RGD.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0032286; P:central nervous system myelin maintenance; IEA:Ensembl.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:0048853; P:forebrain morphogenesis; IEA:Ensembl.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:Ensembl.
GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
GO; GO:0060292; P:long term synaptic depression; IMP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0060179; P:male mating behavior; IEA:Ensembl.
GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
GO; GO:0007613; P:memory; IMP:RGD.
GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0090344; P:negative regulation of cell aging; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl.
GO; GO:0031658; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0051548; P:negative regulation of keratinocyte migration; IEA:Ensembl.
GO; GO:0031642; P:negative regulation of myelination; IEA:Ensembl.
GO; GO:0050765; P:negative regulation of phagocytosis; IMP:RGD.
GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IMP:RGD.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:2000272; P:negative regulation of receptor activity; IMP:RGD.
GO; GO:0090071; P:negative regulation of ribosome biogenesis; IEA:Ensembl.
GO; GO:2000808; P:negative regulation of synaptic vesicle clustering; IEA:Ensembl.
GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IDA:RGD.
GO; GO:0007270; P:neuron-neuron synaptic transmission; IEA:Ensembl.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:RGD.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:1903984; P:positive regulation of TRAIL-activated apoptotic signaling pathway; IEA:Ensembl.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0097107; P:postsynaptic density assembly; IEA:Ensembl.
GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
GO; GO:0097105; P:presynaptic membrane assembly; IEA:Ensembl.
GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IMP:RGD.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
GO; GO:0002902; P:regulation of B cell apoptotic process; IEA:Ensembl.
GO; GO:0033032; P:regulation of myeloid cell apoptotic process; IEA:Ensembl.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
GO; GO:0033198; P:response to ATP; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0010043; P:response to zinc ion; IEP:RGD.
GO; GO:0060024; P:rhythmic synaptic transmission; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IEA:Ensembl.
GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR014020; Tensin_C2-dom.
InterPro; IPR029023; Tensin_phosphatase.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
Pfam; PF00782; DSPc; 1.
Pfam; PF10409; PTEN_C2; 1.
PIRSF; PIRSF038025; PTEN; 1.
SMART; SM01326; PTEN_C2; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS51182; C2_TENSIN; 1.
PROSITE; PS51181; PPASE_TENSIN; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:2K20};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Proteomics identification {ECO:0000213|PeptideAtlas:O54857};
Reference proteome {ECO:0000313|Proteomes:UP000002494}.
DOMAIN 14 185 Phosphatase tensin-type.
{ECO:0000259|PROSITE:PS51181}.
DOMAIN 190 350 C2 tensin-type.
{ECO:0000259|PROSITE:PS51182}.
SEQUENCE 403 AA; 47118 MW; 243BFE35FE209FE5 CRC64;
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK
HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA
AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY
LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKLMY
FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI
DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS
SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHSQI TKV


Related products :

Catalog number Product name Quantity
EIAAB32956 Mmac1,Mouse,Mus musculus,Mutated in multiple advanced cancers 1,Phosphatase and tensin homolog,Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN,Pten
EIAAB32957 Homo sapiens,Human,MMAC1,Mutated in multiple advanced cancers 1,Phosphatase and tensin homolog,Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN,PTEN
EIAAB41949 C1 domain-containing phosphatase and tensin homolog,C1-TEN,Homo sapiens,Human,KIAA1075,TENC1,Tensin-2,Tensin-like C1 domain-containing phosphatase,TNS2
EIAAB32958 Canis familiaris,Canis lupus familiaris,Dog,MMAC1,Mutated in multiple advanced cancers 1,Phosphatase and tensin homolog,Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity prot
EIAAB41948 C1 domain-containing phosphatase and tensin homolog,C1-TEN,Mouse,Mus musculus,Tenc1,Tensin-2,Tensin-like C1 domain-containing phosphatase,Tns2
18-783-78998 GOAT ANTI PTEN - PHOSPHATASE AND TENSIN HOMOLOGUE (MUTATED IN MULTIPLE ADVANCED CANCERS 1) Polyclonal 0.1 mg
18-003-43927 Putative tyrosine-protein phosphatase TPTE - EC 3.1.3.48; Transmembrane phosphatase with tensin homology; Protein BJ-HCC-5; Cancer_testis antigen 44; CT44 Polyclonal 0.1 mg Protein A
orb81290 Human Phosphatase and Tensin homolog His Tag protein Proteins 1
orb81289 Human Phosphatase and Tensin Homolog protein Proteins 2
PTEN11-C Human Phosphatase and tensin homolog (PTEN) protein control for WB 100 ul
PTEN15-R-10 Recombinant purified Human Phosphatase and tensin homolog (PTEN-GST) fusion Protein (full length, GST-tag) 10 ug
PTEN15-R-50 Recombinant purified Human Phosphatase and tensin homolog (PTEN_GST) fusion Protein (full length, GST_tag) 50 ug
PTEN15-R-10 Recombinant purified Human Phosphatase and tensin homolog (PTEN_GST) fusion Protein (full length, GST_tag) 10 ug
EIAAB43667 Cancer_testis antigen 44,CT44,Homo sapiens,Human,Putative tyrosine-protein phosphatase TPTE,TPTE,Transmembrane phosphatase with tensin homology,Tumor antigen BJ-HCC-5
3517 (NT) Phosphatase and tensin homolog 0.5 mg
3515 (CT) Phosphatase and tensin homolog 0.1 mg
3515 (CT) Phosphatase and tensin homolog 0.5 mg
3517 (NT) Phosphatase and tensin homolog 0.1 mg
pro-305 Recombinant Human Phosphatase and Tensin Homolog 10
RPR-712 Recombinant Human Phosphatase and Tensin homolog His Tag 1
pro-305 Recombinant Human Phosphatase and Tensin Homolog 2
pro-712 Recombinant Human Phosphatase and Tensin homolog His Tag 100
pro-712 Recombinant Human Phosphatase and Tensin homolog His Tag 5
PRO-305 Recombinant Human Phosphatase and Tensin Homolog 10µg
PRO-712 Recombinant Human Phosphatase and Tensin homolog His Tag 5µg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur