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SH3 and PX domain-containing protein 2B (Factor for adipocyte differentiation 49) (Tyrosine kinase substrate with four SH3 domains)

 SPD2B_MOUSE             Reviewed;         908 AA.
A2AAY5; B6F0V1; Q1LZL8; Q1LZM5; Q3TB89; Q8BIC6;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
22-NOV-2017, entry version 90.
RecName: Full=SH3 and PX domain-containing protein 2B;
AltName: Full=Factor for adipocyte differentiation 49;
AltName: Full=Tyrosine kinase substrate with four SH3 domains;
Name=Sh3pxd2b; Synonyms=Fad49, Tks4;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN.
PubMed=18959745; DOI=10.1111/j.1742-4658.2008.06682.x;
Hishida T., Eguchi T., Osada S., Nishizuka M., Imagawa M.;
"A novel gene, fad49, plays a crucial role in the immediate early
stage of adipocyte differentiation via involvement in mitotic clonal
expansion.";
FEBS J. 275:5576-5588(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Dendritic cell;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-647.
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-661, AND 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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, 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).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ADAM15.
PubMed=19669234; DOI=10.1007/s00335-009-9210-9;
Mao M., Thedens D.R., Chang B., Harris B.S., Zheng Q.Y., Johnson K.R.,
Donahue L.R., Anderson M.G.;
"The podosomal-adaptor protein SH3PXD2B is essential for normal
postnatal development.";
Mamm. Genome 20:462-475(2009).
[8]
FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF TYR-25;
TYR-373 AND TYR-508, AND SUBCELLULAR LOCATION.
PubMed=19144821; DOI=10.1091/mbc.E08-09-0949;
Buschman M.D., Bromann P.A., Cejudo-Martin P., Wen F., Pass I.,
Courtneidge S.A.;
"The novel adaptor protein Tks4 (SH3PXD2B) is required for functional
podosome formation.";
Mol. Biol. Cell 20:1302-1311(2009).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19755710; DOI=10.1126/scisignal.2000370;
Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A.,
Bokoch G.M.;
"Novel p47(phox)-related organizers regulate localized NADPH oxidase 1
(Nox1) activity.";
Sci. Signal. 2:RA54-RA54(2009).
[10]
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=20137777; DOI=10.1016/j.ajhg.2010.01.009;
Iqbal Z., Cejudo-Martin P., de Brouwer A., van der Zwaag B.,
Ruiz-Lozano P., Scimia M.C., Lindsey J.D., Weinreb R., Albrecht B.,
Megarbane A., Alanay Y., Ben-Neriah Z., Amenduni M., Artuso R.,
Veltman J.A., van Beusekom E., Oudakker A., Millan J.L., Hennekam R.,
Hamel B., Courtneidge S.A., van Bokhoven H.;
"Disruption of the podosome adaptor protein TKS4 (SH3PXD2B) causes the
skeletal dysplasia, eye, and cardiac abnormalities of Frank-Ter Haar
Syndrome.";
Am. J. Hum. Genet. 86:254-261(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-528, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
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 involved in invadopodia and podosome
formation and extracellular matrix degradation. Binds matrix
metalloproteinases (ADAMs), NADPH oxidases (NOXs) and
phosphoinositides. Acts as an organizer protein that allows
NOX1- or NOX3-dependent reactive oxygen species (ROS) generation
and ROS localization. Plays a role in mitotic clonal expansion
during the immediate early stage of adipocyte differentiation.
{ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:19144821,
ECO:0000269|PubMed:19755710}.
-!- SUBUNIT: Interacts with NOXO1 (By similarity). Interacts (via SH3
domains) with NOXA1; the interaction is direct (By similarity).
Interacts with ADAM15. Interacts with FASLG (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome.
Note=Cytoplasmic in normal cells and localizes to podosomes in
SRC-transformed cells.
-!- TISSUE SPECIFICITY: Highly expressed in the stromal-vascular
fraction of white adipose tissue with moderate expression in
heart, skeletal muscle and the mature adipocyte fraction of white
adipose tissue. Also expressed in brain, spleen, kidney and liver.
Expressed in white and brown adipose tissues, eye, lung, heart,
brain, spleen, stomach, liver and skeletal muscle (at protein
level). Not expressed in kidney or bone marrow.
{ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:19144821,
ECO:0000269|PubMed:19669234}.
-!- DEVELOPMENTAL STAGE: Expression increases quickly after induction
of adipocyte differentiation, reaches a maximum after 3 hours and
decreases by 12 hours. Expressed from embryonic day E10.5 in heart
and hindbrain, followed by an increased expression at E12.5 that
also involves a subset of cells on the luminal side of the left
ventricular wall in the case of the heart and neuroepithelium in
the case of the brain. At E14.5, expression is present in
developing bones (proximal ribs, lower jaw and clavicle), but the
expression in the heart is no longer detectable. At stages E16.5
and E18.5, strong expression is seen in the long bones of the
limbs, particularly in the growth plates, as well as in the facial
and cranial bones and the primordial incisor. Expression in the
ribs is seen in the proximal regions in those areas where the
transition from cartilage to bone is expected to occur. Expression
in the eye at E16.5 is highly specific for the ganglion cell
layer. {ECO:0000269|PubMed:18959745, ECO:0000269|PubMed:20137777}.
-!- DOMAIN: The PX domain is required for podosome localization
because of its ability to bind phosphatidylinositol 3-phosphate
(PtdIns(3)P) and phosphatidylinositol 3,4-bisphosphate
(PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-
phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate
(PtdIns(5)P), and phosphatidylinositol 3,5-bisphosphate
(PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylated in SRC-transformed cells.
{ECO:0000269|PubMed:19144821}.
-!- DISRUPTION PHENOTYPE: Exhibit skeletal, cardiac and eye
phenotypes. Mice have glaucoma and suffer growth retardation as
well as craniofacial defects. Skeletons show marked kyphosis,
poorly aligned teeth, anomalies in the iliac crest, and a
prominent xiphisternum. Mice show loss of adipose tissue as well
as cardiac deficiencies, such as dysmorphic ventricular chambers,
thin mitral valves and immature and disarrayed trabeculae with
frequent apical indentation. Mice show loss of ROS formation.
{ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20137777}.
-!- SIMILARITY: Belongs to the SH3PXD2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC40843.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; AB430861; BAG81976.1; -; mRNA.
EMBL; AK089330; BAC40843.1; ALT_FRAME; mRNA.
EMBL; AK171384; BAE42425.1; -; mRNA.
EMBL; AL662780; CAM22517.1; -; Genomic_DNA.
EMBL; BC115711; AAI15712.1; -; mRNA.
EMBL; BC115764; AAI15765.1; -; mRNA.
CCDS; CCDS24526.1; -.
RefSeq; NP_796338.2; NM_177364.3.
UniGene; Mm.227616; -.
ProteinModelPortal; A2AAY5; -.
SMR; A2AAY5; -.
IntAct; A2AAY5; 1.
MINT; MINT-4110712; -.
STRING; 10090.ENSMUSP00000044276; -.
iPTMnet; A2AAY5; -.
PhosphoSitePlus; A2AAY5; -.
MaxQB; A2AAY5; -.
PaxDb; A2AAY5; -.
PeptideAtlas; A2AAY5; -.
PRIDE; A2AAY5; -.
Ensembl; ENSMUST00000038753; ENSMUSP00000044276; ENSMUSG00000040711.
GeneID; 268396; -.
KEGG; mmu:268396; -.
UCSC; uc007ijq.1; mouse.
CTD; 285590; -.
MGI; MGI:2442062; Sh3pxd2b.
eggNOG; KOG4773; Eukaryota.
eggNOG; ENOG410YBFF; LUCA.
GeneTree; ENSGT00530000063010; -.
HOGENOM; HOG000154376; -.
HOVERGEN; HBG107128; -.
InParanoid; A2AAY5; -.
OMA; WFCQVLS; -.
OrthoDB; EOG091G00YX; -.
PhylomeDB; A2AAY5; -.
TreeFam; TF329347; -.
PRO; PR:A2AAY5; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000040711; -.
CleanEx; MM_SH3PXD2B; -.
Genevisible; A2AAY5; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0002102; C:podosome; IDA:UniProtKB.
GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IMP:UniProtKB.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IBA:GO_Central.
GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
GO; GO:0060348; P:bone development; IMP:UniProtKB.
GO; GO:1904888; P:cranial skeletal system development; IMP:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
GO; GO:0001654; P:eye development; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0002051; P:osteoblast fate commitment; IMP:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
GO; GO:0071800; P:podosome assembly; IMP:UniProtKB.
GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
CDD; cd12075; SH3_Tks4_1; 1.
CDD; cd12076; SH3_Tks4_2; 1.
CDD; cd12078; SH3_Tks4_3; 1.
CDD; cd12018; SH3_Tks4_4; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR001683; Phox.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR030512; SH3PXD2B.
InterPro; IPR035477; SH3PXD2B_SH3_1.
InterPro; IPR035478; SH3PXD2B_SH3_2.
InterPro; IPR035479; SH3PXD2B_SH3_3.
InterPro; IPR035480; SH3PXD2B_SH3_4.
PANTHER; PTHR15706:SF2; PTHR15706:SF2; 1.
Pfam; PF00787; PX; 1.
Pfam; PF00018; SH3_1; 3.
Pfam; PF07653; SH3_2; 1.
SMART; SM00312; PX; 1.
SMART; SM00326; SH3; 4.
SUPFAM; SSF50044; SSF50044; 4.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50195; PX; 1.
PROSITE; PS50002; SH3; 4.
1: Evidence at protein level;
Cell junction; Cell projection; Complete proteome; Cytoplasm;
Differentiation; Phosphoprotein; Reference proteome; Repeat;
SH3 domain.
CHAIN 1 908 SH3 and PX domain-containing protein 2B.
/FTId=PRO_0000312202.
DOMAIN 5 129 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 152 211 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 221 280 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 368 427 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 847 908 SH3 4. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COMPBIAS 718 777 Pro-rich.
MOD_RES 25 25 Phosphotyrosine.
{ECO:0000305|PubMed:19144821}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000250|UniProtKB:A1X283}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:A1X283}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 661 661 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 840 840 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MUTAGEN 25 25 Y->F: Reduced phosphorylation. Almost
complete loss of phosphorylation; when
associated with F-373 and F-508.
{ECO:0000269|PubMed:19144821}.
MUTAGEN 373 373 Y->F: Reduced phosphorylation. Almost
complete loss of phosphorylation; when
associated with F-25 and F-508.
{ECO:0000269|PubMed:19144821}.
MUTAGEN 508 508 Y->F: Reduced phosphorylation. Almost
complete loss of phosphorylation; when
associated with F-25 and F-373.
{ECO:0000269|PubMed:19144821}.
CONFLICT 464 464 V -> M (in Ref. 1; BAG81976 and 4;
AAI15765). {ECO:0000305}.
CONFLICT 744 744 V -> VSV (in Ref. 1; BAG81976 and 2;
BAE42425). {ECO:0000305}.
CONFLICT 749 749 L -> Q (in Ref. 1; BAG81976 and 2;
BAE42425). {ECO:0000305}.
SEQUENCE 908 AA; 101517 MW; 83341ABA6DF639AB CRC64;
MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGATEA IYRRYSKFFD LQMQMLDKFP
MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE YCKALIQLPP YISQCDEVLQ
FFETRPEDLN PPKEEHIGKK KSGNDPTSVD PMVLEQYVVV ADYQKQESSE ISLSVGQVVD
IIEKNESGWW FVSTAEEQGW VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM
NLERGAVVEV VQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKLGPS SPAHSGALDL
DGVSRHQNAM GREKELLNNQ RDGRFEGRLV PDGDVKQRSP KMRQRPPPRR DMTIPRGLNL
PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK SLSGWWYIQM EDKEGWAPAT
FIDKYKKTSS ASRPNFLAPL PHEMTQLRLG DAAATENNTG PEAVGPSRPL PEAPHGAVDS
GMLWSKDWKG GKEAPRKASS DLSASTGYEE ISDPTQEEKP SLPPRKESII KSEEELLERE
RQKMEPLRGS SPKPPGMILP MIPAKHAPLA RDSRKPEPKL DKSKFPLRND MGLECGHKVL
AKEVKKPNLR PISRSKAELS EEKVDPTSQN LFMKSRPQVR PKPTPSPKTE PAQSEDHVDI
YNLRSKLRPA KSQEKALLDG ESHHAAGSHD TALSRSFLPG EGPGHGQDRS GRQDGLSPKE
TPCRAPPRPA KTTDPGPKNV PVPVQEATLQ QRPVVPPRRP PPPKKTSSSP LSCRPLPEVR
GAQREESRVA PAAGRALLVP PKAKPFLSNS SVGQDDMRGK GGLGPRVTGK VGETREKAAS
FLNADGPKDS LYVAVANFEG DEDTSSFQEG TVFEVREKNS SGWWFCQVLS GAPSWEGWIP
SNYLRKKP


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E0147h ELISA kit FLT,FLT1,FLT-1,Fms-like tyrosine kinase 1,FRT,Homo sapiens,Human,Tyrosine-protein kinase FRT,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,Vascular perm 96T
U0147h CLIA FLT,FLT1,FLT-1,Fms-like tyrosine kinase 1,FRT,Homo sapiens,Human,Tyrosine-protein kinase FRT,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,Vascular permeabili 96T
10-782-55028 Discoidin domain-containing receptor 2 - EC 2.7.10.1; Discoidin domain receptor 2; Receptor protein-tyrosine kinase TKT; Tyrosine-protein kinase TYRO 10; Neurotrophic tyrosine kinase. receptor-related 0.001 mg
10-782-55028 Discoidin domain-containing receptor 2 - EC 2.7.10.1; Discoidin domain receptor 2; Receptor protein-tyrosine kinase TKT; Tyrosine-protein kinase TYRO 10; Neurotrophic tyrosine kinase. receptor-related 0.005 mg
10-782-55028 Discoidin domain-containing receptor 2 - EC 2.7.10.1; Discoidin domain receptor 2; Receptor protein-tyrosine kinase TKT; Tyrosine-protein kinase TYRO 10; Neurotrophic tyrosine kinase. receptor-related 0.01 mg
10-782-55028 Discoidin domain-containing receptor 2 - EC 2.7.10.1; Discoidin domain receptor 2; Receptor protein-tyrosine kinase TKT; Tyrosine-protein kinase TYRO 10; Neurotrophic tyrosine kinase. receptor-related 0.02 mg
U0605m CLIA 30 kDa adipocyte complement-related protein,Acdc,ACRP30,Acrp30,Adipocyte complement-related 30 kDa protein,Adipocyte, C1q and collagen domain-containing protein,Adipocyte-specific protein AdipoQ, 96T
E0605m ELISA 30 kDa adipocyte complement-related protein,Acdc,ACRP30,Acrp30,Adipocyte complement-related 30 kDa protein,Adipocyte, C1q and collagen domain-containing protein,Adipocyte-specific protein AdipoQ 96T
E0148h ELISA kit Fetal liver kinase 1,FLK1,FLK-1,Homo sapiens,Human,KDR,Kinase insert domain receptor,Protein-tyrosine kinase receptor flk-1,Vascular endothelial growth factor receptor 2,VEGFR-2 96T
U0148h CLIA Fetal liver kinase 1,FLK1,FLK-1,Homo sapiens,Human,KDR,Kinase insert domain receptor,Protein-tyrosine kinase receptor flk-1,Vascular endothelial growth factor receptor 2,VEGFR-2 96T
E0148h ELISA Fetal liver kinase 1,FLK1,FLK-1,Homo sapiens,Human,KDR,Kinase insert domain receptor,Protein-tyrosine kinase receptor flk-1,Vascular endothelial growth factor receptor 2,VEGFR-2 96T
orb70965 pp60 (v-SRC) Autophosphorylation Site,Protein Tyrosine Kinase Substrate peptide This is pp60 (v-SRC) Autophosphorylation Site,Protein Tyrosine Kinase Substrate peptide. For research use only. 1 mg
E0605m ELISA kit 30 kDa adipocyte complement-related protein,Acdc,ACRP30,Acrp30,Adipocyte complement-related 30 kDa protein,Adipocyte, C1q and collagen domain-containing protein,Adipocyte-specific protein A 96T
10-663-45256 Adiponectin (Acrp30) Mouse - Adipocyte. C1q and collagen domain-containing protein; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipocyte-specific 0.02 mg
10-663-45256 Adiponectin (Acrp30) Mouse - Adipocyte. C1q and collagen domain-containing protein; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipocyte-specific 0.1 mg
10-663-45256 Adiponectin (Acrp30) Mouse - Adipocyte. C1q and collagen domain-containing protein; 30 kDa adipocyte complement-related protein; Adipocyte complement-related 30 kDa protein; ACRP30; Adipocyte-specific 1 mg
E1915m ELISA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T


 

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