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Protein crumbs homolog 2 (crumbs2) (Crumbs-like protein 2)

 CRUM2_MOUSE             Reviewed;        1282 AA.
Q80YA8; A2ALU1; Q6P6N1;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 3.
28-FEB-2018, entry version 134.
RecName: Full=Protein crumbs homolog 2 {ECO:0000305};
Short=crumbs2 {ECO:0000303|PubMed:26496195};
AltName: Full=Crumbs-like protein 2;
Flags: Precursor;
Name=Crb2 {ECO:0000312|MGI:MGI:2679260};
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 [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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-1282.
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
TISSUE SPECIFICITY.
PubMed=15851977;
van den Hurk J.A.J.M., Rashbass P., Roepman R., Davis J.,
Voesenek K.E.J., Arends M.L., Zonneveld M.N., van Roekel M.H.G.,
Cameron K., Rohrschneider K., Heckenlively J.R., Koenekoop R.K.,
Hoyng C.B., Cremers F.P.M., den Hollander A.I.;
"Characterization of the crumbs homolog 2 (CRB2) gene and analysis of
its role in retinitis pigmentosa and Leber congenital amaurosis.";
Mol. Vis. 11:263-273(2005).
[4]
DISRUPTION PHENOTYPE.
PubMed=22072575; DOI=10.1002/dvdy.22778;
Xiao Z., Patrakka J., Nukui M., Chi L., Niu D., Betsholtz C.,
Pikkarainen T., Pikkarainan T., Vainio S., Tryggvason K.;
"Deficiency in Crumbs homolog 2 (Crb2) affects gastrulation and
results in embryonic lethality in mice.";
Dev. Dyn. 240:2646-2656(2011).
[5]
DISRUPTION PHENOTYPE.
PubMed=23001562; DOI=10.1093/hmg/dds398;
Alves C.H., Sanz A.S., Park B., Pellissier L.P., Tanimoto N.,
Beck S.C., Huber G., Murtaza M., Richard F., Sridevi Gurubaran I.,
Garcia Garrido M., Levelt C.N., Rashbass P., Le Bivic A.,
Seeliger M.W., Wijnholds J.;
"Loss of CRB2 in the mouse retina mimics human retinitis pigmentosa
due to mutations in the CRB1 gene.";
Hum. Mol. Genet. 22:35-50(2013).
[6]
GLYCOSYLATION AT SER-271, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=26496195; DOI=10.1371/journal.pgen.1005551;
Ramkumar N., Harvey B.M., Lee J.D., Alcorn H.L., Silva-Gagliardi N.F.,
McGlade C.J., Bestor T.H., Wijnholds J., Haltiwanger R.S.,
Anderson K.V.;
"Protein O-glucosyltransferase 1 (POGLUT1) promotes mouse gastrulation
through modification of the apical polarity protein CRUMBS2.";
PLoS Genet. 11:E1005551-E1005551(2015).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=27870829; DOI=10.1038/ncb3442;
Ramkumar N., Omelchenko T., Silva-Gagliardi N.F., McGlade C.J.,
Wijnholds J., Anderson K.V.;
"Crumbs2 promotes cell ingression during the epithelial-to-mesenchymal
transition at gastrulation.";
Nat. Cell Biol. 18:1281-1291(2016).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26802325; DOI=10.1016/j.neures.2016.01.001;
Dudok J.J., Murtaza M., Henrique Alves C., Rashbass P., Wijnholds J.;
"Crumbs 2 prevents cortical abnormalities in mouse dorsal
telencephalon.";
Neurosci. Res. 108:12-23(2016).
-!- FUNCTION: Apical polarity protein that plays a central role during
the epithelial-to-mesenchymal transition (EMT) at gastrulation,
when newly specified mesodermal cells move inside the embryo
(PubMed:26496195, PubMed:27870829). Acts by promoting cell
ingression, the process by which cells leave the epithelial
epiblast and move inside the embryo to form a new tissue layer
(PubMed:27870829). The anisotropic distribution of CRB2 and
MYH10/myosin-IIB at cell edges define which cells will ingress:
cells with high apical CRB2 are probably extruded from the
epiblast by neighboring cells with high levels of apical
MYH10/myosin-IIB (PubMed:27870829). Also required for maintenance
of the apical polarity complex during development of the cortex.
{ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:26802325,
ECO:0000269|PubMed:27870829}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:27870829};
Single-pass type I membrane protein {ECO:0000255}. Note=O-
glucosylation is required for localization at the apical plasma
membrane (PubMed:26496195). Distributed in a complex anisotropic
pattern on apical cell edges: the level of CRB2 on a cell edge is
inversely correlated with the level of MYH10/myosin-IIB
(PubMed:27870829). {ECO:0000269|PubMed:26496195,
ECO:0000269|PubMed:27870829}.
-!- TISSUE SPECIFICITY: In the adult eye, strongly expressed in the
outer nuclear layer, containing the cell bodies of the
photoreceptor cells, and in the inner nuclear layer, containing
the cell bodies of the horizontal, bipolar, amacrine, and Mueller
glial cells (PubMed:15851977). Also expressed in some cells in the
ganglion cell layer (or may be displaced amacrine cells rather
than ganglion cells) (PubMed:15851977).
{ECO:0000269|PubMed:15851977}.
-!- DEVELOPMENTAL STAGE: Expressed in early embryonic cells, more
specifically in embryonic regions undergoing dramatic
rearrangement, such as the developing neuroepithelium which
proceeds with neural tube closure, the anterior splitting lateral
plate mesoderm that wraps the pericardial cavity and the
differentiating somite epithelium. Widely expressed throughout the
epiblast and the lateral plate mesoderm at embryonic day 7 (E7).
At E7.5-E7.75, continues to be expressed in these regions, and
expression is also found on the apical side of the embryonic
endoderm, and extraembryonic amnion and allantois. At E8-E8.5,
expression is also detected in the heart tube, foregut and the
apical side of the somite epithelium. Stronger expression is
detected on the apical sides of the splitting lateral plate
mesoderm, and the apical side of the neural ectoderm at trunk
region. Not expressed in the notochord plate or the extra-
embryonic endoderm. {ECO:0000269|PubMed:22072575}.
-!- PTM: O-glucosylated by POGLUT1 at Ser-271; consists of an O-
glucose trisaccharide, in which the O-glucose is elongated by the
addition of two xylose residues (PubMed:26496195). O-glucosylation
is required for localization at the plasma membrane
(PubMed:26496195). {ECO:0000269|PubMed:26496195}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality due impaired
gastrulation (PubMed:22072575, PubMed:27870829). Mesoderm
formation is disrupted, and cells do not ingress
(PubMed:27870829). Instead, a single layer forms, and the embryo
fails to properly establish its body plan, leading to embryonic
arrest (PubMed:27870829). Conditional deletion in the developing
retina leads to progressive disorganization during late retinal
development: retina show progressive thinning of the photoreceptor
layer and sites of cellular mislocalization (PubMed:23001562).
Conditional deletion in the dorsal telencephalon leads to defects
in the maintenance of the apical complex (PubMed:26802325).
{ECO:0000269|PubMed:22072575, ECO:0000269|PubMed:23001562,
ECO:0000269|PubMed:26802325, ECO:0000269|PubMed:27870829}.
-!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
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EMBL; AL805959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC043114; AAH43114.1; -; mRNA.
EMBL; BC062128; AAH62128.1; -; mRNA.
CCDS; CCDS50580.1; -.
RefSeq; NP_001157038.1; NM_001163566.1.
UniGene; Mm.392369; -.
ProteinModelPortal; Q80YA8; -.
SMR; Q80YA8; -.
STRING; 10090.ENSMUSP00000058007; -.
iPTMnet; Q80YA8; -.
PhosphoSitePlus; Q80YA8; -.
MaxQB; Q80YA8; -.
PaxDb; Q80YA8; -.
PeptideAtlas; Q80YA8; -.
PRIDE; Q80YA8; -.
Ensembl; ENSMUST00000050372; ENSMUSP00000058007; ENSMUSG00000035403.
GeneID; 241324; -.
KEGG; mmu:241324; -.
UCSC; uc008jnf.2; mouse.
CTD; 286204; -.
MGI; MGI:2679260; Crb2.
eggNOG; KOG1217; Eukaryota.
eggNOG; ENOG410XP6K; LUCA.
GeneTree; ENSGT00910000144018; -.
HOGENOM; HOG000230899; -.
HOVERGEN; HBG080001; -.
InParanoid; Q80YA8; -.
KO; K16681; -.
OMA; PFCGQNT; -.
OrthoDB; EOG091G00O4; -.
PhylomeDB; Q80YA8; -.
TreeFam; TF316224; -.
PRO; PR:Q80YA8; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000035403; -.
CleanEx; MM_CRB2; -.
ExpressionAtlas; Q80YA8; baseline and differential.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0072358; P:cardiovascular system development; IMP:UniProtKB.
GO; GO:0055111; P:ingression involved in gastrulation with mouth forming second; IMP:UniProtKB.
GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:UniProtKB.
GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
GO; GO:0014028; P:notochord formation; IMP:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
GO; GO:0001756; P:somitogenesis; IMP:UniProtKB.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001791; Laminin_G.
Pfam; PF00008; EGF; 9.
Pfam; PF12661; hEGF; 1.
Pfam; PF02210; Laminin_G_2; 1.
SMART; SM00181; EGF; 15.
SMART; SM00179; EGF_CA; 13.
SMART; SM00282; LamG; 3.
SUPFAM; SSF49899; SSF49899; 4.
SUPFAM; SSF57184; SSF57184; 3.
PROSITE; PS00010; ASX_HYDROXYL; 8.
PROSITE; PS00022; EGF_1; 14.
PROSITE; PS01186; EGF_2; 9.
PROSITE; PS50026; EGF_3; 15.
PROSITE; PS01187; EGF_CA; 5.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
Calcium; Cell membrane; Complete proteome; Developmental protein;
Disulfide bond; EGF-like domain; Gastrulation; Glycoprotein; Membrane;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 1282 Protein crumbs homolog 2. {ECO:0000255}.
/FTId=PRO_0000055626.
TOPO_DOM 36 1221 Extracellular. {ECO:0000305}.
TRANSMEM 1222 1242 Helical. {ECO:0000255}.
TOPO_DOM 1243 1282 Cytoplasmic. {ECO:0000305}.
DOMAIN 71 110 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 112 148 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 150 186 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 188 225 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 227 263 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 265 322 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 324 360 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 362 398 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 400 440 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 444 607 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 609 645 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 649 808 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 810 846 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 872 1051 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1053 1089 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1091 1127 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1131 1168 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1170 1206 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 O-linked (Glc...) serine.
{ECO:0000305|PubMed:26496195}.
CARBOHYD 442 442 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 672 672 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 693 693 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 789 789 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 803 803 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 839 839 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 889 889 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 929 929 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1006 1006 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1138 1138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1155 1155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 86 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 80 98 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 100 109 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 116 127 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 121 136 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 138 147 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 154 165 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 159 174 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 176 185 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 192 203 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 197 212 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 214 224 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 231 242 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 236 251 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 253 262 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 269 280 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 274 310 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 312 321 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 328 339 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 333 348 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 350 359 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 366 377 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 371 386 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 388 397 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 404 415 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 409 428 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 430 439 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 583 607 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 613 624 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 618 633 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 635 644 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 769 808 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 814 825 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 819 834 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 836 845 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1010 1051 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 1057 1068 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1062 1077 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1079 1088 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1095 1105 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1100 1115 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1117 1126 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1135 1147 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1141 1156 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1158 1167 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1174 1185 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1179 1194 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1196 1205 {ECO:0000255|PROSITE-ProRule:PRU00076}.
CONFLICT 842 842 G -> E (in Ref. 2; AAH62128).
{ECO:0000305}.
SEQUENCE 1282 AA; 134760 MW; 9099A9AAD1FEC403 CRC64;
MALVGPRIWG PRRDIYPLLL LLLLLLLLLL PWVPAGLVPP ETPSVCASDP CAPGTKCQAT
ESGGYTCEPS ELGGCATQPC HHGALCVPQG PDPNSFRCYC VPGFQGPHCE LDIDECASRP
CQHGGTCQNL ADHYECHCPL GYAGVTCEAE VDECSSAPCL HGGSCLDGVG SYRCVCAPGY
AGANCQLDVD ECQSQPCAHG GVCHDLVNGF RCDCADTGYE GARCEQEVLE CASAPCAHNA
SCLDGFRSFR CLCWPGFSGE RCEVDEDECA SGPCQNGGQC LQRSDPTLYG GVQAIFPGAF
SFSHAAGFLC SCPLGFAGND CSMDVDECAS GPCLNGGSCQ DLPNGFQCYC QDGYTGLTCQ
EDMDECQSEP CLHGGTCSDT VAGYICQCPE AWGGHDCSVQ LTGCQGHTCP LAATCIPTFK
SGLHGYFCRC PPGTYGPFCG QNTTFSVVSG SSVWGLVPAA ASLGLALRFR TTLLAGTLAT
LKDTRDSLEL VLVGAVLQAT LSRHGTAVLI LTLPDLALND GHWHQVEVTL HLGTLELRLW
HEGCPGQLCV ASGPVATGPT ASVASGPPGS YSIYLGGGVF AGCFQDVRVE GHLLLPEELK
GTVLLGCERR EPCQPLPCAH GGACVDLWTH FRCDCPRPYR GATCTDEVPA ATFGLGGATS
SASFLLHQLG PNLTVSFFLR TREPAGLLLQ FANDSVASLT VFLSEGQIRA EGLGHPAVVL
PGRWDDGLPH LVMLSFGPDQ LQDLGQRLYV GGRFYPDDTQ LWGGPFRGCL QDLQLNSIHL
PFFSSPMENS SWPSELEAGQ SSNLTQGCVS EDTCNPNPCF NGGTCHVTWN DFYCTCSENF
TGPTCAQQRW CPRQPCLPPA TCEEVPDGFV CVAEATFREG PPAVFTGHNV SSSLSGLTLA
FRTRDSEAGL LRAVSAAGAH SNIWLAVRNG SLAGDVAGSV LPAPGPRVAD GAWHRVRLAR
EFPQAAASRW LLWLDGAATP VALHGLGGDL GFLQGPGAVP LLLAENFTGC LGRVALGDFP
LPLAPPRSGT VSGAREHFVA WPGSPAVSLG CRGGPVCSPS PCLHGGACRD LFDAFACSCG
PAWEGPRCEI RADPCRSTPC VRGQCHARPD GRFECRCPPG FSGPRCRLPV LPQGCNLNST
CKDGAPCEGG PLGTNCSCQE GLAGLRCQSL DKPCEASPCL NGGTCRVASG IFECTCSAGF
SGQFCEVVKT LPLPLPFPLL EVAVPAACAC LLLLLLGLLS GILAARKRRQ SEGTYSPSQQ
EVAGARLEMD SVLKVPPEER LI


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