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Multiple epidermal growth factor-like domains protein 10 (Multiple EGF-like domains protein 10)

 MEG10_MOUSE             Reviewed;        1147 AA.
Q6DIB5; Q3TLU3; Q3UG73;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
25-OCT-2017, entry version 123.
RecName: Full=Multiple epidermal growth factor-like domains protein 10 {ECO:0000312|MGI:MGI:2685177};
Short=Multiple EGF-like domains protein 10;
Flags: Precursor;
Name=Megf10 {ECO:0000312|MGI:MGI:2685177};
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 MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, AND DEVELOPMENTAL STAGE.
PubMed=17205124; DOI=10.1371/journal.pone.0000120;
Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
Zhou Z., Chimini G.;
"Cooperation between engulfment receptors: the case of ABCA1 and
MEGF10.";
PLoS ONE 1:E120-E120(2006).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
Suzuki E., Nakayama M.;
"MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
assembly protein complex 2 medium chain and induces large vacuole
formation.";
Exp. Cell Res. 313:3729-3742(2007).
[5]
FUNCTION IN MYOGENESIS, AND TISSUE SPECIFICITY.
PubMed=18056409; DOI=10.1083/jcb.200709083;
Holterman C.E., Le Grand F., Kuang S., Seale P., Rudnicki M.A.;
"Megf10 regulates the progression of the satellite cell myogenic
program.";
J. Cell Biol. 179:911-922(2007).
[6]
FUNCTION IN ENDOCYTOSIS.
PubMed=20828568; DOI=10.1016/j.febslet.2010.08.050;
Singh T.D., Park S.Y., Bae J.S., Yun Y., Bae Y.C., Park R.W.,
Kim I.S.;
"MEGF10 functions as a receptor for the uptake of amyloid-beta.";
FEBS Lett. 584:3936-3942(2010).
[7]
FUNCTION IN NEURONAL MOSAIC SPACING.
PubMed=22407321; DOI=10.1038/nature10877;
Kay J.N., Chu M.W., Sanes J.R.;
"MEGF10 and MEGF11 mediate homotypic interactions required for mosaic
spacing of retinal neurons.";
Nature 483:465-469(2012).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27170117; DOI=10.1523/JNEUROSCI.3850-15.2016;
Iram T., Ramirez-Ortiz Z., Byrne M.H., Coleman U.A., Kingery N.D.,
Means T.K., Frenkel D., El Khoury J.;
"Megf10 Is a Receptor for C1Q That Mediates Clearance of Apoptotic
Cells by Astrocytes.";
J. Neurosci. 36:5185-5192(2016).
[9]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION
WITH NOTCH1.
PubMed=28498977; DOI=10.1093/hmg/ddx189;
Saha M., Mitsuhashi S., Jones M.D., Manko K., Reddy H.M., Bruels C.,
Cho K.A., Pacak C.A., Draper I., Kang P.B.;
"Consequences of MEGF10 deficiency on myoblast function and Notch1
interactions.";
Hum. Mol. Genet. 26:2984-3000(2017).
-!- FUNCTION: Membrane receptor involved in phagocytosis by
macrophages and astrocytes of apoptotic cells. Receptor for C1q,
an eat-me signal, that binds phosphatidylserine expressed on the
surface of apoptotic cells (PubMed:27170117). Cooperates with
ABCA1 within the process of engulfment (By similarity). Promotes
the formation of large intracellular vacuoles and may be
responsible for the uptake of amyloid-beta peptides
(PubMed:20828568). Necessary for astrocyte-dependent apoptotic
neuron clearance in the developing cerebellum (PubMed:27170117).
Plays role in muscle cell proliferation, adhesion and motility. Is
also an essential factor in the regulation of myogenesis. Controls
the balance between skeletal muscle satellite cells proliferation
and differentiation through regulation of the notch signaling
pathway (PubMed:28498977). May also function in the mosaic spacing
of specific neuron subtypes in the retina through homotypic
retinal neuron repulsion. Mosaics provide a mechanism to
distribute each cell type evenly across the retina, ensuring that
all parts of the visual field have access to a full set of
processing elements (PubMed:22407321).
{ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:18056409,
ECO:0000269|PubMed:20828568, ECO:0000269|PubMed:22407321,
ECO:0000269|PubMed:27170117, ECO:0000269|PubMed:28498977}.
-!- SUBUNIT: Homopolymer (Probable). Interacts with GULP1 and ABCA1.
Interacts with AP2M1. Does not interact with MEGF11 (By
similarity). Binds with high affinity to complement C1q (By
similarity). Interacts (via the cytoplasmic domain) with NOTCH1
(via NICD domain) (PubMed:28498977).
{ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:28498977,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17643423,
ECO:0000269|PubMed:28498977}; Single-pass type I membrane protein
{ECO:0000269|PubMed:17643423}. Cell projection, phagocytic cup
{ECO:0000250|UniProtKB:Q96KG7}. Note=Forms an irregular, mosaic-
like adhesion pattern in region of the cell surface that becomes
firmely fixed to the substrate. Expressed at the cell surface in
clusters around cell corpses during engulfment. During the
engulfment of apoptotic thymocytes, recruited at the bottom of the
forming phagocytic cup. Colocalizes with ABCA1 in absence of any
phagocytic challenge. Does not localize within lamellipodia. Does
not localize with MEGF11 (By similarity). Enriched at the sites of
contact with apoptotic thymocyte cells.
{ECO:0000250|UniProtKB:Q96KG7}.
-!- TISSUE SPECIFICITY: Expressed in cerebellum (at protein level).
Expressed in kidney, stellate cells of the cerebellum and
macrophage cell lines. {ECO:0000269|PubMed:17205124,
ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:18056409}.
-!- DEVELOPMENTAL STAGE: Expressed in embryo at 15 dpc (at protein
level). Expressed in embryo at 8, 10, 11, 13, 14 and 15 dpc.
{ECO:0000269|PubMed:17205124}.
-!- DOMAIN: The EMI and EGF-like domains work in concert to promote
self-assembly.
-!- PTM: Ubiquitinated; mono- and polyubiquitinated forms are
detected. {ECO:0000250|UniProtKB:Q96KG7}.
-!- PTM: Phosphorylated on tyrosine residues. Phosphorylation at Tyr-
1030 may be important for muscle cell proliferation.
{ECO:0000250|UniProtKB:Q96KG7}.
-!- DISRUPTION PHENOTYPE: Mutants show at postnatal day 7 an increased
amount of apoptotic cells in the developing cerebellum. However,
adult brains do not show higher numbers of apoptotic cells in the
cerebellum compared to wild-type. Astrocytes from knockout mice as
well as heterozigous mice have a significant impairment in
engulfment of apoptotic cells (PubMed:27170117). Mutants have
normal mobility and their skeletal muscles show mildly increased
endomysial connective tissue. They display reduced motor activity
after exercise and show slower muscle regeneration
(PubMed:28498977). MEGF10 and DMD double knockout animals have
pronounced fiber size variability and intracellular inclusions in
the quadriceps femoris with extensive endomysial connective tissue
infiltration. Mice develop muscle weakness, kyphosis and a
waddling gait. At 2 months of age, they have reduced contractile
force compared to wild-type mice. They display reduced motor
activity after exercise and they walk shorter distances than wild-
type. They have a delayed regeneration after muscle injury and an
aberrant muscle fber typing and cross-sectional areas
(PubMed:28498977). {ECO:0000269|PubMed:27170117,
ECO:0000269|PubMed:28498977}.
-!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK147238; BAE27788.1; -; mRNA.
EMBL; AK148084; BAE28336.1; -; mRNA.
EMBL; AK166316; BAE38699.1; -; mRNA.
EMBL; BC075647; AAH75647.1; -; mRNA.
CCDS; CCDS29264.1; -.
RefSeq; NP_001001979.1; NM_001001979.2.
UniGene; Mm.297863; -.
ProteinModelPortal; Q6DIB5; -.
SMR; Q6DIB5; -.
STRING; 10090.ENSMUSP00000075174; -.
iPTMnet; Q6DIB5; -.
PhosphoSitePlus; Q6DIB5; -.
MaxQB; Q6DIB5; -.
PaxDb; Q6DIB5; -.
PeptideAtlas; Q6DIB5; -.
PRIDE; Q6DIB5; -.
Ensembl; ENSMUST00000075770; ENSMUSP00000075174; ENSMUSG00000024593.
GeneID; 70417; -.
KEGG; mmu:70417; -.
UCSC; uc008eyz.2; mouse.
CTD; 84466; -.
MGI; MGI:2685177; Megf10.
eggNOG; KOG1218; Eukaryota.
eggNOG; ENOG410XQWV; LUCA.
GeneTree; ENSGT00730000110380; -.
HOGENOM; HOG000294130; -.
HOVERGEN; HBG108333; -.
InParanoid; Q6DIB5; -.
OMA; FGCNLTC; -.
OrthoDB; EOG091G00XN; -.
PhylomeDB; Q6DIB5; -.
TreeFam; TF332598; -.
ChiTaRS; Megf10; mouse.
PRO; PR:Q6DIB5; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024593; -.
CleanEx; MM_MEGF10; -.
ExpressionAtlas; Q6DIB5; baseline and differential.
Genevisible; Q6DIB5; MM.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0001891; C:phagocytic cup; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001849; F:complement component C1q binding; ISO:MGI.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
GO; GO:1902742; P:apoptotic process involved in development; IMP:MGI.
GO; GO:0043652; P:engulfment of apoptotic cell; IMP:MGI.
GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
GO; GO:0055001; P:muscle cell development; ISS:UniProtKB.
GO; GO:0033002; P:muscle cell proliferation; ISO:MGI.
GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
GO; GO:0043654; P:recognition of apoptotic cell; IDA:MGI.
GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB.
GO; GO:0048641; P:regulation of skeletal muscle tissue development; ISO:MGI.
GO; GO:0014719; P:skeletal muscle satellite cell activation; IMP:UniProtKB.
GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:UniProtKB.
GO; GO:0014841; P:skeletal muscle satellite cell proliferation; IDA:UniProtKB.
Gene3D; 1.20.5.100; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR011489; EMI_domain.
InterPro; IPR002049; Laminin_EGF.
Pfam; PF12661; hEGF; 8.
Pfam; PF00053; Laminin_EGF; 6.
SMART; SM00181; EGF; 17.
SMART; SM00180; EGF_Lam; 14.
PROSITE; PS00022; EGF_1; 17.
PROSITE; PS01186; EGF_2; 17.
PROSITE; PS50026; EGF_3; 15.
PROSITE; PS51041; EMI; 1.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Cell projection; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Myogenesis;
Phagocytosis; Phosphoprotein; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1147 Multiple epidermal growth factor-like
domains protein 10.
/FTId=PRO_0000309733.
TOPO_DOM 26 857 Extracellular. {ECO:0000255}.
TRANSMEM 858 878 Helical. {ECO:0000255}.
TOPO_DOM 879 1147 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 107 EMI. {ECO:0000255|PROSITE-
ProRule:PRU00384}.
DOMAIN 101 136 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 144 179 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 187 222 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 230 265 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 278 308 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 316 351 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 405 440 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 453 483 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 491 526 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 539 569 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 577 612 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 665 700 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 713 743 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 751 786 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 799 829 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 1 857 Necessary for interaction with AP2M1,
self-assembly and formation of the
irregular, mosaic-like adhesion pattern.
{ECO:0000250|UniProtKB:Q96KG7}.
REGION 945 1147 Necessary for formation of large
intracellular vacuoles.
{ECO:0000250|UniProtKB:Q96KG7}.
COMPBIAS 1119 1146 Ser-rich.
MOD_RES 1030 1030 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q96KG7}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 95 {ECO:0000255}.
DISULFID 60 69 {ECO:0000255}.
DISULFID 94 105 {ECO:0000255}.
DISULFID 109 124 {ECO:0000250}.
DISULFID 126 135 {ECO:0000250}.
DISULFID 148 160 {ECO:0000250}.
DISULFID 154 167 {ECO:0000250}.
DISULFID 169 178 {ECO:0000250}.
DISULFID 191 203 {ECO:0000250}.
DISULFID 197 210 {ECO:0000250}.
DISULFID 212 221 {ECO:0000250}.
DISULFID 234 246 {ECO:0000250}.
DISULFID 240 253 {ECO:0000250}.
DISULFID 255 264 {ECO:0000250}.
DISULFID 281 289 {ECO:0000250}.
DISULFID 283 296 {ECO:0000250}.
DISULFID 298 307 {ECO:0000250}.
DISULFID 320 332 {ECO:0000250}.
DISULFID 326 339 {ECO:0000250}.
DISULFID 341 350 {ECO:0000250}.
DISULFID 409 421 {ECO:0000250}.
DISULFID 415 428 {ECO:0000250}.
DISULFID 430 439 {ECO:0000250}.
DISULFID 456 464 {ECO:0000250}.
DISULFID 458 471 {ECO:0000250}.
DISULFID 473 482 {ECO:0000250}.
DISULFID 495 507 {ECO:0000250}.
DISULFID 501 514 {ECO:0000250}.
DISULFID 516 525 {ECO:0000250}.
DISULFID 542 550 {ECO:0000250}.
DISULFID 544 557 {ECO:0000250}.
DISULFID 559 568 {ECO:0000250}.
DISULFID 581 593 {ECO:0000250}.
DISULFID 587 600 {ECO:0000250}.
DISULFID 602 611 {ECO:0000250}.
DISULFID 669 681 {ECO:0000250}.
DISULFID 675 688 {ECO:0000250}.
DISULFID 690 699 {ECO:0000250}.
DISULFID 716 724 {ECO:0000250}.
DISULFID 718 731 {ECO:0000250}.
DISULFID 733 742 {ECO:0000250}.
DISULFID 755 767 {ECO:0000250}.
DISULFID 761 774 {ECO:0000250}.
DISULFID 776 785 {ECO:0000250}.
DISULFID 802 810 {ECO:0000250}.
DISULFID 804 817 {ECO:0000250}.
DISULFID 819 828 {ECO:0000250}.
CONFLICT 323 323 A -> T (in Ref. 1; BAE38699).
{ECO:0000305}.
CONFLICT 1092 1092 G -> S (in Ref. 1; BAE38699).
{ECO:0000305}.
CONFLICT 1137 1137 N -> S (in Ref. 1; BAE38699).
{ECO:0000305}.
CONFLICT 1140 1140 S -> T (in Ref. 1; BAE38699).
{ECO:0000305}.
SEQUENCE 1147 AA; 122972 MW; FBC50896096181CC CRC64;
MAISSSSCLG LICSLLCHWV GTASSLNLED PNVCSHWESY SVTVQESYPH PFDQIYYTSC
TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE SRDMCVPHCA DKCVHGRCIA
PNTCQCEPGW GGTNCSSACD GDHWGPHCSS RCQCKNRALC NPITGACHCA AGYRGWRCED
RCEQGTYGND CHQRCQCQNG ATCDHITGEC RCSPGYTGAF CEDLCPPGKH GPHCEQRCPC
QNGGVCHHVT GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP
GYTGERCQDE CPVGSYGVRC AEACRCVNGG KCYHVSGTCL CEAGFSGELC EARLCPEGLY
GIKCDKRCPC HLDNTHSCHP MSGECGCKPG WSGLYCNETC SPGFYGEACQ QICSCQNGAD
CDSVTGRCAC APGFKGTDCS TPCPLGRYGI NCSSRCGCKN DAVCSPVDGS CICKAGWHGV
DCSIRCPSGT WGFGCNLTCQ CLNGGACNTL DGTCTCAPGW RGAKCEFPCQ DGTYGLNCAE
RCDCSHADGC HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC
ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG FTGALCNEVC
PSGRFGKNCA GVCTCTNNGT CNPIDRSCQC YPGWIGSDCS QPCPPAHWGP NCIHTCNCHN
GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF YGKDCALICQ CQNGADCDHI SGQCTCRTGF
MGRHCEQKCP AGTYGYGCRQ ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN
SLSRTSTALP ADSYQIGAIA GIVVLVLVVL FLLALFIIYR HKQKRKESSM PAVTYTPAMR
VINADYTIAE TLPHSNGGNA NSHYFTNPSY HTLSQCATSP HVNNRDRMTI AKSKNNQLFV
NLKNVNPGKR GTLVDCTGTL PADWKQGGYL NELGAFGLDR SYMGKSLKDL GKNSEYNSST
CSLSSSENPY ATIKDPPALL PKSSECGYVE MKSPARRDSP YAEINNSTPA NRNVYEVEPT
VSVVQGVFSN SGHVTQDPYD LPKNSHIPCH YDLLPVRDSS SSPKREDGGG SNSTSSNSTS
SSSSSSE


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EIAAB12603 Egfl7,EGF-like protein 7,Epidermal growth factor-like protein 7,Megf7,Mouse,Multiple EGF-like domains protein 7,Multiple epidermal growth factor-like domains protein 7,Mus musculus,NOTCH4-like protein
EIAAB14452 Cadherin family member 8,CDHF8,FAT2,hFat2,Homo sapiens,Human,KIAA0811,MEGF1,Multiple EGF-like domains protein 1,Multiple epidermal growth factor-like domains protein 1,Protocadherin Fat 2
EIAAB38673 Homo sapiens,Human,KIAA0814,MEGF5,Multiple EGF-like domains protein 5,Multiple epidermal growth factor-like domains protein 5,SLIL2,Slit homolog 3 protein,SLIT3,Slit-3,UNQ691_PRO1336
EIAAB38670 Homo sapiens,Human,KIAA0813,MEGF4,Multiple EGF-like domains protein 4,Multiple epidermal growth factor-like domains protein 4,SLIL1,Slit homolog 1 protein,SLIT1,Slit-1
EIAAB38674 Megf5,Multiple EGF-like domains protein 5,Multiple epidermal growth factor-like domains protein 5,Rat,Rattus norvegicus,Slit homolog 3 protein,Slit3,Slit-3
EIAAB38671 Megf4,Multiple EGF-like domains protein 4,Multiple epidermal growth factor-like domains protein 4,Rat,Rattus norvegicus,Slit homolog 1 protein,Slit1,Slit-1
25-807 INADL is a protein with multiple PDZ domains. PDZ domains mediate protein-protein interactions, and proteins with multiple PDZ domains often organize multimeric complexes at the plasma membrane. This 0.05 mg
TRM2A_MOUSE Rat ELISA Kit FOR Multiple epidermal growth factor-like domains protein 8 96T
E0590Ge Rat ELISA Kit FOR Multiple epidermal growth factor-like domains protein 8 96T
E15038h Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 10 96T
CSB-EL013680RA Rat Multiple epidermal growth factor-like domains protein 6(MEGF6) ELISA kit 96T
MEGF8_HUMAN Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 8 96T
CSB-EL013681RA Rat Multiple epidermal growth factor-like domains protein 8(MEGF8) ELISA kit 96T
TRI25_HUMAN Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 6 96T
TRPC7_MOUSE Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 11 96T
E0589h Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 6 96T
E0589Rb Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 11 96T
CSB-EL013681MO Mouse Multiple epidermal growth factor-like domains protein 8(MEGF8) ELISA kit 96T


 

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