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GRB2-associated-binding protein 2 (GRB2-associated binder 2) (Growth factor receptor bound protein 2-associated protein 2) (pp100)

 GAB2_HUMAN              Reviewed;         676 AA.
Q9UQC2; A2RRM2; A6NEW9; A7MD36; O60317;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-NOV-2018, entry version 153.
RecName: Full=GRB2-associated-binding protein 2;
AltName: Full=GRB2-associated binder 2;
AltName: Full=Growth factor receptor bound protein 2-associated protein 2;
AltName: Full=pp100;
Name=GAB2; Synonyms=KIAA0571;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PTPN11.
TISSUE=Myeloma;
PubMed=10068651;
Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T.,
Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.;
"Gab-family adapter proteins act downstream of cytokine and growth
factor receptors and T- and B-cell antigen receptors.";
Blood 93:1809-1816(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[3]
SEQUENCE REVISION.
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
[7]
PHOSPHORYLATION BY HCK, AND INTERACTION WITH HCK; CRKL PTPN11 AND
GRB2.
PubMed=15010462; DOI=10.1074/jbc.M305783200;
Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T.,
Catley L.P., Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.;
"Critical role for hematopoietic cell kinase (Hck)-mediated
phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-
induced proliferation and survival of multiple myeloma cells.";
J. Biol. Chem. 279:21658-21665(2004).
[8]
FUNCTION, AND INTERACTION WITH TNFRSF11A.
PubMed=15750601; DOI=10.1038/nm1203;
Wada T., Nakashima T., Oliveira-dos-Santos A.J., Gasser J., Hara H.,
Schett G., Penninger J.M.;
"The molecular scaffold Gab2 is a crucial component of RANK signaling
and osteoclastogenesis.";
Nat. Med. 11:394-399(2005).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR; GRB2; PTPN11;
PI-3 KINASE; SFN; SHC1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAQ AND YWHAZ,
MUTAGENESIS OF SER-210 AND THR-391, AND PHOSPHORYLATION AT SER-133;
SER-140; SER-141; SER-148; SER-149; SER-159; SER-164; SER-210;
SER-218; SER-223; SER-264; THR-278; SER-281; THR-287; TYR-293;
THR-331; THR-385; THR-391; SER-405; SER-480; SER-543; SER-622 AND
SER-623.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-148; SER-149;
SER-223; SER-264; SER-285; THR-287; SER-368; THR-391; SER-422;
SER-425; SER-543 AND TYR-643, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 350-358 IN COMPLEX WITH
GRB2, AND X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 508-522 IN COMPLEX
WITH GRB2.
PubMed=19523899; DOI=10.1016/j.str.2009.03.017;
Harkiolaki M., Tsirka T., Lewitzky M., Simister P.C., Joshi D.,
Bird L.E., Jones E.Y., O'Reilly N., Feller S.M.;
"Distinct binding modes of two epitopes in Gab2 that interact with the
SH3C domain of Grb2.";
Structure 17:809-822(2009).
-!- FUNCTION: Adapter protein which acts downstream of several
membrane receptors including cytokine, antigen, hormone, cell
matrix and growth factor receptors to regulate multiple signaling
pathways. Regulates osteoclast differentiation mediating the
TNFRSF11A/RANK signaling. In allergic response, it plays a role in
mast cells activation and degranulation through PI-3-kinase
regulation. Also involved in the regulation of cell proliferation
and hematopoiesis. {ECO:0000269|PubMed:15750601,
ECO:0000269|PubMed:19172738}.
-!- SUBUNIT: Interacts with SHC1; may mediate interaction with
receptors (By similarity). Interacts with SYK (By similarity).
Interacts with PI-3 kinase. Interacts with GRB2 (via SH3 2
domain). Interacts (phosphorylated) with PTPN11. Interacts with
TNFRSF11A (via cytoplasmic domain). Interacts (phosphorylated)
with 14-3-3 family proteins SFN, YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ
and YWHAZ; prevents interaction with GRB2 and attenuates GAB2
signaling. Interacts with HCK. {ECO:0000250,
ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:15010462,
ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738,
ECO:0000269|PubMed:19523899}.
-!- INTERACTION:
P62993:GRB2; NbExp=10; IntAct=EBI-975200, EBI-401755;
P62993-1:GRB2; NbExp=3; IntAct=EBI-15787947, EBI-15787932;
Q06124:PTPN11; NbExp=4; IntAct=EBI-975200, EBI-297779;
P31946:YWHAB; NbExp=4; IntAct=EBI-975200, EBI-359815;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19172738}.
Cell membrane {ECO:0000269|PubMed:19172738}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UQC2-1; Sequence=Displayed;
Name=2;
IsoId=Q9UQC2-2; Sequence=VSP_038520;
-!- DOMAIN: The SH3-binding motifs mediate interaction with SHC1 and
GRB2. {ECO:0000250}.
-!- DOMAIN: The PH domain mediates phosphatidylinositol 3,4,5-
trisphosphate and phosphatidylinositol 3,4-bisphosphate binding.
{ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residue(s) by the thrombopoietin
receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and
B-cell antigen receptors, gp130, IL-2R and IL-3R (By similarity).
Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL
(By similarity). Phosphorylated upon EGF stimulation.
Phosphorylated on tyrosine residues by HCK upon IL6 signaling.
{ECO:0000250, ECO:0000269|PubMed:15010462,
ECO:0000269|PubMed:19172738}.
-!- PTM: Dephosphorylated by PTPN11.
-!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA25497.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GAB2ID40664ch11q14.html";
-----------------------------------------------------------------------
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EMBL; AB018413; BAA76737.1; -; mRNA.
EMBL; AB011143; BAA25497.2; ALT_INIT; mRNA.
EMBL; AP002985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW75057.1; -; Genomic_DNA.
EMBL; CH471076; EAW75058.1; -; Genomic_DNA.
EMBL; BC131711; AAI31712.1; -; mRNA.
EMBL; BC152459; AAI52460.1; -; mRNA.
CCDS; CCDS8259.1; -. [Q9UQC2-1]
CCDS; CCDS8260.1; -. [Q9UQC2-2]
RefSeq; NP_036428.1; NM_012296.3. [Q9UQC2-2]
RefSeq; NP_536739.1; NM_080491.2. [Q9UQC2-1]
RefSeq; XP_006718816.1; XM_006718753.2. [Q9UQC2-2]
UniGene; Hs.429434; -.
PDB; 2VWF; X-ray; 1.58 A; B=508-522.
PDB; 2W0Z; X-ray; 1.70 A; B=350-358.
PDB; 5EWZ; X-ray; 2.34 A; C=387-395, D=207-212.
PDB; 5EXA; X-ray; 1.95 A; C/D=387-396.
PDBsum; 2VWF; -.
PDBsum; 2W0Z; -.
PDBsum; 5EWZ; -.
PDBsum; 5EXA; -.
ProteinModelPortal; Q9UQC2; -.
SMR; Q9UQC2; -.
BioGrid; 115181; 73.
DIP; DIP-36653N; -.
IntAct; Q9UQC2; 15.
MINT; Q9UQC2; -.
STRING; 9606.ENSP00000354952; -.
iPTMnet; Q9UQC2; -.
PhosphoSitePlus; Q9UQC2; -.
BioMuta; GAB2; -.
DMDM; 46396035; -.
EPD; Q9UQC2; -.
PaxDb; Q9UQC2; -.
PeptideAtlas; Q9UQC2; -.
PRIDE; Q9UQC2; -.
ProteomicsDB; 85541; -.
ProteomicsDB; 85542; -. [Q9UQC2-2]
Ensembl; ENST00000340149; ENSP00000343959; ENSG00000033327. [Q9UQC2-2]
Ensembl; ENST00000361507; ENSP00000354952; ENSG00000033327. [Q9UQC2-1]
GeneID; 9846; -.
KEGG; hsa:9846; -.
UCSC; uc001ozg.4; human. [Q9UQC2-1]
CTD; 9846; -.
DisGeNET; 9846; -.
EuPathDB; HostDB:ENSG00000033327.12; -.
GeneCards; GAB2; -.
HGNC; HGNC:14458; GAB2.
HPA; CAB022159; -.
HPA; HPA000271; -.
HPA; HPA001368; -.
MIM; 606203; gene.
neXtProt; NX_Q9UQC2; -.
OpenTargets; ENSG00000033327; -.
PharmGKB; PA28478; -.
eggNOG; ENOG410IEDA; Eukaryota.
eggNOG; ENOG4111RDE; LUCA.
GeneTree; ENSGT00510000046662; -.
HOGENOM; HOG000236270; -.
HOVERGEN; HBG051685; -.
InParanoid; Q9UQC2; -.
KO; K08091; -.
OMA; ENYVAMQ; -.
OrthoDB; EOG091G03BY; -.
PhylomeDB; Q9UQC2; -.
TreeFam; TF329487; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-8983432; Interleukin-15 signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; Q9UQC2; -.
SIGNOR; Q9UQC2; -.
ChiTaRS; GAB2; human.
EvolutionaryTrace; Q9UQC2; -.
GeneWiki; GAB2; -.
GenomeRNAi; 9846; -.
PRO; PR:Q9UQC2; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000033327; Expressed in 216 organ(s), highest expression level in inferior vagus X ganglion.
CleanEx; HS_GAB2; -.
ExpressionAtlas; Q9UQC2; baseline and differential.
Genevisible; Q9UQC2; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0043306; P:positive regulation of mast cell degranulation; ISS:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Membrane; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 676 GRB2-associated-binding protein 2.
/FTId=PRO_0000050285.
DOMAIN 6 117 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOTIF 351 358 SH3-binding.
MOTIF 510 519 SH3-binding.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19172738}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19172738}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19172738}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19172738}.
MOD_RES 265 265 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
MOD_RES 266 266 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
MOD_RES 278 278 Phosphothreonine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 287 287 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19172738}.
MOD_RES 293 293 Phosphotyrosine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 331 331 Phosphothreonine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 385 385 Phosphothreonine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 391 391 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19172738}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 408 408 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 452 452 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9Z1S8}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19172738}.
MOD_RES 622 622 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000269|PubMed:19172738}.
MOD_RES 643 643 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 38 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9628581}.
/FTId=VSP_038520.
VARIANT 320 320 P -> L (in dbSNP:rs752597583).
/FTId=VAR_053097.
VARIANT 344 344 P -> L (in dbSNP:rs2279374).
/FTId=VAR_020407.
MUTAGEN 210 210 S->A,E: Impaired interaction with 14-3-3
proteins and increased EGF-independent
cell proliferation; when associated with
A-391. {ECO:0000269|PubMed:19172738}.
MUTAGEN 391 391 T->A,E: Impaired interaction with 14-3-3
proteins and increased EGF-independent
cell proliferation; when associated with
A-210. {ECO:0000269|PubMed:19172738}.
HELIX 515 517 {ECO:0000244|PDB:2VWF}.
SEQUENCE 676 AA; 74458 MW; 107623FD07D884C9 CRC64;
MSGGGDVVCT GWLRKSPPEK KLRRYAWKKR WFILRSGRMS GDPDVLEYYK NDHSKKPLRI
INLNFCEQVD AGLTFNKKEL QDSFVFDIKT SERTFYLVAE TEEDMNKWVQ SICQICGFNQ
AEESTDSLRN VSSAGHGPRS SPAELSSSSQ HLLRERKSSA PSHSSQPTLF TFEPPVSNHM
QPTLSTSAPQ EYLYLHQCIS RRAENARSAS FSQGTRASFL MRSDTAVQKL AQGNGHCVNG
ISGQVHGFYS LPKPSRHNTE FRDSTYDLPR SLASHGHTKG SLTGSETDNE DVYTFKTPSN
TLCREFGDLL VDNMDVPATP LSAYQIPRTF TLDKNHNAMT VATPGDSAIA PPPRPPKPSQ
AETPRWGSPQ QRPPISENSR SVAATIPRRN TLPAMDNSRL HRASSCETYE YPQRGGESAG
RSAESMSDGV GSFLPGKMIV GRSDSTNSED NYVPMNPGSS TLLAMERAGD NSQSVYIPMS
PGAHHFDSLG YPSTTLPVHR GPSRGSEIQP PPVNRNLKPD RKAKPTPLDL RNNTVIDELP
FKSPITKSWS RANHTFNSSS SQYCRPISTQ SITSTDSGDS EENYVPMQNP VSASPVPSGT
NSPAPKKSTG SVDYLALDFQ PSSPSPHRKP STSSVTSDEK VDYVQVDKEK TQALQNTMQE
WTDVRQSSEP SKGAKL


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E02G0247 Rat Growth Factor Receptor Bound Protein 2 ELISA , Grb2
GRD1 GRB2 Gene growth factor receptor-bound protein 2
E92514Hu ELISA Kit for Growth Factor Receptor Bound Protein 2 (Grb2) 96T/Kit
CD19 Human Growth Factor Receptor-Bound Protein 2 GRB2 l0
E-EL-R0467 Rat GRB2 (Growth Factor Receptor Bound Protein 2) ELISA Kit 96T
E02G0247 Rat Growth Factor Receptor Bound Protein 2 Elisa Kit (Grb2) 96 Tests/kit
CSB-EL009889RA Rat Growth factor receptor-bound protein 2(GRB2) ELISA kit 96T
pro-678 Recombinant Human Growth Factor Receptor-Bound Protein 2 GRB2 1mg
pro-678 Recombinant Human Growth Factor Receptor-Bound Protein 2 GRB2 25
pro-678 Recombinant Human Growth Factor Receptor-Bound Protein 2 GRB2 5


 

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