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Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase 53 kDa substrate)

 BAIP2_MOUSE             Reviewed;         535 AA.
Q8BKX1; Q91V97; Q923V9; Q923W0;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 2.
20-JUN-2018, entry version 143.
RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
Short=BAI-associated protein 2;
Short=BAI1-associated protein 2;
AltName: Full=Insulin receptor substrate protein of 53 kDa;
Short=IRSp53;
Short=Insulin receptor substrate p53;
AltName: Full=Insulin receptor tyrosine kinase 53 kDa substrate;
Name=Baiap2;
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] (ISOFORMS 2 AND 4).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=11514062; DOI=10.1016/S0304-3940(01)02064-X;
Thomas E.A., Foye P.E., Alvarez C.E., Usui H., Sutcliffe J.G.;
"Insulin receptor substrate protein p53 localization in rats suggests
mechanism for specific polyglutamine neurodegeneration.";
Neurosci. Lett. 309:145-148(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 4).
PubMed=12884081; DOI=10.1007/s10038-003-0047-x;
Miyahara A., Okumura-Oho Y., Miyashita T., Hoshika A., Yamada M.;
"Genomic structure and alternative splicing of the insulin receptor
tyrosine kinase substrate of 53-kDa protein.";
J. Hum. Genet. 48:410-414(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH DIAPH1.
PubMed=10814512; DOI=10.1006/bbrc.2000.2671;
Fujiwara T., Mammoto A., Kim Y., Takai Y.;
"Rho small G-protein-dependent binding of mDia to an Src homology 3
domain-containing IRSp53/BAIAP2.";
Biochem. Biophys. Res. Commun. 271:626-629(2000).
[6]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=12006592; DOI=10.1074/jbc.M202512200;
Alvarez C.E., Sutcliffe J.G., Thomas E.A.;
"Novel isoform of insulin receptor substrate p53/p58 is generated by
alternative splicing in the CRIB/SH3-binding region.";
J. Biol. Chem. 277:24728-24734(2002).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
FUNCTION, AND INTERACTION WITH EPS8.
PubMed=17115031; DOI=10.1038/ncb1502;
Disanza A., Mantoani S., Hertzog M., Gerboth S., Frittoli E.,
Steffen A., Berhoerster K., Kreienkamp H.J., Milanesi F.,
Di Fiore P.P., Ciliberto A., Stradal T.E., Scita G.;
"Regulation of cell shape by Cdc42 is mediated by the synergic actin-
bundling activity of the Eps8-IRSp53 complex.";
Nat. Cell Biol. 8:1337-1347(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Kidney;
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).
-!- FUNCTION: Adapter protein that links membrane-bound small G-
proteins to cytoplasmic effector proteins. Necessary for CDC42-
mediated reorganization of the actin cytoskeleton and for RAC1-
mediated membrane ruffling. Involved in the regulation of the
actin cytoskeleton by WASF family members and the Arp2/3 complex.
Plays a role in neurite growth. Acts syngeristically with ENAH to
promote filipodia formation. Plays a role in the reorganization of
the actin cytoskeleton in response to bacterial infection.
Participates in actin bundling when associated with EPS8,
promoting filopodial protrusions. {ECO:0000269|PubMed:17115031}.
-!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been
activated by GTP binding. Binds DIAPH1. Interacts with ATN1,
ADGRB1, SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts
with ENAH after recruitment of CDC42 (By similarity). Interacts
with EPS8. {ECO:0000250, ECO:0000269|PubMed:10814512,
ECO:0000269|PubMed:17115031}.
-!- INTERACTION:
O08808:Diaph1; NbExp=3; IntAct=EBI-771498, EBI-1026445;
Q62108:Dlg4; NbExp=4; IntAct=EBI-771498, EBI-300895;
A4GZ26:Iqsec2; NbExp=7; IntAct=EBI-771498, EBI-8526464;
Q4ACU6:Shank3; NbExp=2; IntAct=EBI-771498, EBI-771450;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell
projection, filopodium {ECO:0000250}. Cell projection, ruffle
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Note=Detected throughout the cytoplasm in the absence of specific
binding partners. Detected in filopodia and close to membrane
ruffles. Recruited to actin pedestals that are formed upon
infection by bacteria at bacterial attachment sites (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8BKX1-1; Sequence=Displayed;
Name=2;
IsoId=Q8BKX1-2; Sequence=VSP_015508;
Name=3;
IsoId=Q8BKX1-3; Sequence=VSP_015509;
Name=4; Synonyms=Short form;
IsoId=Q8BKX1-4; Sequence=VSP_015507, VSP_015508;
-!- TISSUE SPECIFICITY: Detected in liver, brain, olfactory bulb,
brain cortex, caudate putamen, hypothalamus and cerebellum.
{ECO:0000269|PubMed:12006592}.
-!- DOMAIN: The IMD domain forms a coiled coil. The isolated domain
can induce actin bundling and filopodia formation. In the absence
of G-proteins intramolecular interaction between the IMD and the
SH3 domain gives rise to an auto-inhibited state of the protein.
Interaction of the IMD with RAC1 or CDC42 leads to activation (By
similarity). {ECO:0000250}.
-!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2,
SHANK1, DIAPH1 and ENAH. {ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues by INSR in response to
insulin treatment. {ECO:0000250}.
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EMBL; AF390178; AAK68153.1; -; mRNA.
EMBL; AF390179; AAK81838.1; -; mRNA.
EMBL; AB105196; BAC65241.1; -; Genomic_DNA.
EMBL; AB105196; BAC65242.1; -; Genomic_DNA.
EMBL; AK049469; BAC33764.1; -; mRNA.
EMBL; BC006620; AAH06620.1; -; mRNA.
EMBL; BC016411; AAH16411.1; -; mRNA.
CCDS; CCDS25722.1; -. [Q8BKX1-1]
CCDS; CCDS25723.1; -. [Q8BKX1-4]
CCDS; CCDS25724.1; -. [Q8BKX1-2]
RefSeq; NP_001032843.1; NM_001037754.3. [Q8BKX1-4]
RefSeq; NP_001032844.2; NM_001037755.3. [Q8BKX1-1]
RefSeq; NP_570932.2; NM_130862.4. [Q8BKX1-2]
UniGene; Mm.197534; -.
ProteinModelPortal; Q8BKX1; -.
SMR; Q8BKX1; -.
BioGrid; 223833; 11.
DIP; DIP-32392N; -.
IntAct; Q8BKX1; 14.
MINT; Q8BKX1; -.
STRING; 10090.ENSMUSP00000026436; -.
iPTMnet; Q8BKX1; -.
PhosphoSitePlus; Q8BKX1; -.
PaxDb; Q8BKX1; -.
PeptideAtlas; Q8BKX1; -.
PRIDE; Q8BKX1; -.
DNASU; 108100; -.
Ensembl; ENSMUST00000026436; ENSMUSP00000026436; ENSMUSG00000025372. [Q8BKX1-1]
Ensembl; ENSMUST00000075180; ENSMUSP00000074674; ENSMUSG00000025372. [Q8BKX1-2]
Ensembl; ENSMUST00000103021; ENSMUSP00000099310; ENSMUSG00000025372. [Q8BKX1-4]
Ensembl; ENSMUST00000106231; ENSMUSP00000101838; ENSMUSG00000025372. [Q8BKX1-3]
GeneID; 108100; -.
KEGG; mmu:108100; -.
UCSC; uc007mrh.1; mouse. [Q8BKX1-4]
UCSC; uc007mri.1; mouse. [Q8BKX1-1]
CTD; 10458; -.
MGI; MGI:2137336; Baiap2.
eggNOG; ENOG410IKMM; Eukaryota.
eggNOG; ENOG41110CD; LUCA.
GeneTree; ENSGT00390000005995; -.
HOGENOM; HOG000038005; -.
HOVERGEN; HBG054462; -.
InParanoid; Q8BKX1; -.
KO; K05627; -.
OMA; EDYSPWA; -.
OrthoDB; EOG091G05ZV; -.
PhylomeDB; Q8BKX1; -.
TreeFam; TF325648; -.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
ChiTaRS; Baiap2; mouse.
PRO; PR:Q8BKX1; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000025372; -.
ExpressionAtlas; Q8BKX1; baseline and differential.
Genevisible; Q8BKX1; MM.
GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; ISO:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0061846; C:dendritic spine cytoplasm; ISO:MGI.
GO; GO:0060076; C:excitatory synapse; ISO:MGI.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0061845; C:neuron projection branch point; ISO:MGI.
GO; GO:0044306; C:neuron projection terminus; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0098794; C:postsynapse; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0098793; C:presynapse; ISO:MGI.
GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; ISO:MGI.
GO; GO:0097060; C:synaptic membrane; ISO:MGI.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; ISO:MGI.
GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0001221; F:transcription cofactor binding; ISO:MGI.
GO; GO:0051764; P:actin crosslink formation; IMP:UniProtKB.
GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
GO; GO:0016358; P:dendrite development; IMP:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0035418; P:protein localization to synapse; ISO:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; TAS:MGI.
CDD; cd11915; SH3_Irsp53; 1.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR013606; I-BAR_dom.
InterPro; IPR030128; IRSp53.
InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
InterPro; IPR035594; Irsp53_SH3.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR14206; PTHR14206; 1.
PANTHER; PTHR14206:SF3; PTHR14206:SF3; 1.
Pfam; PF08397; IMD; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51338; IMD; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
SH3 domain.
CHAIN 1 535 Brain-specific angiogenesis inhibitor 1-
associated protein 2.
/FTId=PRO_0000064817.
DOMAIN 1 250 IMD. {ECO:0000255|PROSITE-
ProRule:PRU00668}.
DOMAIN 375 438 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 88 153 {ECO:0000255}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 341 341 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 361 361 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQB8}.
VAR_SEQ 290 329 Missing (in isoform 4).
{ECO:0000303|PubMed:11514062}.
/FTId=VSP_015507.
VAR_SEQ 513 535 RNPFANVHLKPTVTNDRSAPLLS -> SGSGTLVSTV (in
isoform 2 and isoform 4).
{ECO:0000303|PubMed:11514062}.
/FTId=VSP_015508.
VAR_SEQ 514 535 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015509.
CONFLICT 87 88 QN -> HI (in Ref. 3; BAC33764).
{ECO:0000305}.
CONFLICT 326 326 S -> F (in Ref. 3; BAC33764).
{ECO:0000305}.
CONFLICT 330 330 S -> F (in Ref. 3; BAC33764).
{ECO:0000305}.
SEQUENCE 535 AA; 59237 MW; 45B4C660FBB07F72 CRC64;
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG
ELASESQGSK ELGDVLFQMA EVHRQIQNQL EETLKSFHNE LLTQLEQKVE LDSRYLSAAL
KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS
DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA
VQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP KNSYATTENK
TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE
KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLALPPP DYGTSSRAFP
TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSRNPFANVH LKPTVTNDRS APLLS


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ABP-PAB-00014 Insulin receptor tyrosin kinase substrate (LOC55971) polyclonal antibody 100 ug
EIAAB13303 Epidermal growth factor receptor kinase substrate 8-like protein 3,Epidermal growth factor receptor pathway substrate 8-related protein 3,Eps8l3,EPS8-like protein 3,Eps8r3,EPS8-related protein 3,Mouse
EIAAB13302 Epidermal growth factor receptor kinase substrate 8-like protein 3,Epidermal growth factor receptor pathway substrate 8-related protein 3,EPS8L3,EPS8-like protein 3,EPS8R3,EPS8-related protein 3,Homo
EIAAB13301 Epidermal growth factor receptor kinase substrate 8-like protein 2,Epidermal growth factor receptor pathway substrate 8-related protein 2,EPS8L2,EPS8-like protein 2,EPS8R2,EPS8-related protein 2,Homo
EIAAB13300 Epidermal growth factor receptor kinase substrate 8-like protein 2,Epidermal growth factor receptor pathway substrate 8-related protein 2,Eps8l2,EPS8-like protein 2,Eps8r2,EPS8-related protein 2,Mouse
EIAAB13299 Epidermal growth factor receptor kinase substrate 8-like protein 1,Epidermal growth factor receptor pathway substrate 8-related protein 1,Eps8l1,EPS8-like protein 1,Eps8r1,EPS8-related protein 1,Mouse
EIAAB13298 DRC3,Epidermal growth factor receptor kinase substrate 8-like protein 1,Epidermal growth factor receptor pathway substrate 8-related protein 1,EPS8L1,EPS8-like protein 1,EPS8R1,EPS8-related protein 1,
orb70982 Protein Kinase C Substrate from EGF Receptor peptide This is Protein Kinase C Substrate from EGF Receptor peptide. For research use only. 1 mg
E02I0406 Rat Insulin receptor substrate 2 96 Tests/kit
E02I0406 Rat Insulin receptor substrate 2 ELISA, IRS-2 96 Tests/kit
E02I0406 Rat Insulin receptor substrate 2 ELISA 96T/kit
E03I0406 Mouse Insulin receptor substrate 2 96 Tests/kit
YHB0581Ra Rat Insulin receptor substrate 1,IRS-1 ELISA Kit 96T


 

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