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Multiple epidermal growth factor-like domains protein 8 (Multiple EGF-like domains protein 8) (Epidermal growth factor-like protein 4) (EGF-like protein 4)

 MEGF8_HUMAN             Reviewed;        2845 AA.
Q7Z7M0; A8KAY0; O75097;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
22-NOV-2017, entry version 149.
RecName: Full=Multiple epidermal growth factor-like domains protein 8;
Short=Multiple EGF-like domains protein 8;
AltName: Full=Epidermal growth factor-like protein 4;
Short=EGF-like protein 4;
Flags: Precursor;
Name=MEGF8; Synonyms=C19orf49, EGFL4, KIAA0817;
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 2).
TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[2]
SEQUENCE REVISION.
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 416-2845 (ISOFORM 1).
Shan Y.X., Yu L.;
"Cloning, characterization and location of a novel human gene
containing an EGF domain.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1271.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[7]
VARIANTS CRPT2 ARG-199; HIS-1566 AND GLY-2434.
PubMed=23063620; DOI=10.1016/j.ajhg.2012.08.027;
Twigg S.R., Lloyd D., Jenkins D., Elcioglu N.E., Cooper C.D.,
Al-Sannaa N., Annagur A., Gillessen-Kaesbach G., Huning I.,
Knight S.J., Goodship J.A., Keavney B.D., Beales P.L., Gileadi O.,
McGowan S.J., Wilkie A.O.;
"Mutations in multidomain protein MEGF8 identify a Carpenter syndrome
subtype associated with defective lateralization.";
Am. J. Hum. Genet. 91:897-905(2012).
-!- INTERACTION:
O15265:ATXN7; NbExp=2; IntAct=EBI-947617, EBI-708350;
O00555:CACNA1A; NbExp=2; IntAct=EBI-947617, EBI-766279;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7Z7M0-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z7M0-2; Sequence=VSP_036067;
-!- DISEASE: Carpenter syndrome 2 (CRPT2) [MIM:614976]: An autosomal
recessive multiple congenital malformation disorder characterized
by multisuture craniosynostosis and polysyndactyly of the hands
and feet, in association with abnormal left-right patterning and
other features, most commonly obesity, umbilical hernia,
cryptorchidism, and congenital heart disease.
{ECO:0000269|PubMed:23063620}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAP35084.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA32469.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB011541; BAA32469.2; ALT_INIT; mRNA.
EMBL; AC011497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC024078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC153880; AAI53881.1; -; mRNA.
EMBL; AY280362; AAP35084.1; ALT_INIT; mRNA.
CCDS; CCDS12604.2; -. [Q7Z7M0-2]
CCDS; CCDS62693.1; -. [Q7Z7M0-1]
PIR; T00209; T00209.
RefSeq; NP_001258867.1; NM_001271938.1. [Q7Z7M0-1]
RefSeq; NP_001401.2; NM_001410.2. [Q7Z7M0-2]
UniGene; Hs.132483; -.
ProteinModelPortal; Q7Z7M0; -.
SMR; Q7Z7M0; -.
BioGrid; 108274; 13.
IntAct; Q7Z7M0; 10.
MINT; MINT-2808456; -.
STRING; 9606.ENSP00000334219; -.
iPTMnet; Q7Z7M0; -.
PhosphoSitePlus; Q7Z7M0; -.
BioMuta; MEGF8; -.
DMDM; 218511690; -.
EPD; Q7Z7M0; -.
PaxDb; Q7Z7M0; -.
PeptideAtlas; Q7Z7M0; -.
PRIDE; Q7Z7M0; -.
Ensembl; ENST00000251268; ENSP00000251268; ENSG00000105429. [Q7Z7M0-1]
Ensembl; ENST00000334370; ENSP00000334219; ENSG00000105429. [Q7Z7M0-2]
GeneID; 1954; -.
KEGG; hsa:1954; -.
UCSC; uc002otl.4; human. [Q7Z7M0-1]
CTD; 1954; -.
DisGeNET; 1954; -.
EuPathDB; HostDB:ENSG00000105429.12; -.
GeneCards; MEGF8; -.
HGNC; HGNC:3233; MEGF8.
HPA; HPA049248; -.
MalaCards; MEGF8; -.
MIM; 604267; gene.
MIM; 614976; phenotype.
neXtProt; NX_Q7Z7M0; -.
OpenTargets; ENSG00000105429; -.
Orphanet; 65759; Carpenter syndrome.
PharmGKB; PA27666; -.
eggNOG; KOG1388; Eukaryota.
eggNOG; ENOG410YF0N; LUCA.
GeneTree; ENSGT00390000001118; -.
HOGENOM; HOG000113554; -.
HOVERGEN; HBG108128; -.
InParanoid; Q7Z7M0; -.
OMA; TREGKCM; -.
OrthoDB; EOG091G0030; -.
PhylomeDB; Q7Z7M0; -.
TreeFam; TF321873; -.
SignaLink; Q7Z7M0; -.
ChiTaRS; MEGF8; human.
GenomeRNAi; 1954; -.
PRO; PR:Q7Z7M0; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105429; -.
CleanEx; HS_MEGF8; -.
ExpressionAtlas; Q7Z7M0; baseline and differential.
Genevisible; Q7Z7M0; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0097094; P:craniofacial suture morphogenesis; IMP:UniProtKB.
GO; GO:0071907; P:determination of digestive tract left/right asymmetry; ISS:UniProtKB.
GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:UniProtKB.
GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:UniProtKB.
GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:UniProtKB.
GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProtKB.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IMP:UniProtKB.
GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:UniProtKB.
GO; GO:0060972; P:left/right pattern formation; IMP:UniProtKB.
GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
CDD; cd00041; CUB; 1.
Gene3D; 2.120.10.80; -; 1.
Gene3D; 2.130.10.80; -; 3.
Gene3D; 2.60.120.290; -; 2.
InterPro; IPR000859; CUB_dom.
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; IPR024731; EGF_dom.
InterPro; IPR037293; Gal_Oxidase_b-propeller.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR002165; Plexin_repeat.
InterPro; IPR016201; PSI.
InterPro; IPR035914; Sperma_CUB_dom_sf.
Pfam; PF00431; CUB; 1.
Pfam; PF12947; EGF_3; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00053; Laminin_EGF; 3.
Pfam; PF01437; PSI; 1.
SMART; SM00042; CUB; 1.
SMART; SM00181; EGF; 13.
SMART; SM00179; EGF_CA; 2.
SMART; SM00180; EGF_Lam; 4.
SMART; SM00423; PSI; 9.
SUPFAM; SSF117281; SSF117281; 3.
SUPFAM; SSF49854; SSF49854; 1.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01180; CUB; 2.
PROSITE; PS00022; EGF_1; 6.
PROSITE; PS01186; EGF_2; 7.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01248; EGF_LAM_1; 4.
PROSITE; PS50027; EGF_LAM_2; 4.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Craniosynostosis;
Disease mutation; Disulfide bond; EGF-like domain; Glycoprotein;
Kelch repeat; Laminin EGF-like domain; Membrane; Phosphoprotein;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 2845 Multiple epidermal growth factor-like
domains protein 8.
/FTId=PRO_0000055629.
TOPO_DOM 28 2647 Extracellular. {ECO:0000255}.
TRANSMEM 2648 2668 Helical. {ECO:0000255}.
TOPO_DOM 2669 2845 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 140 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 138 168 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 170 203 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 241 287 Kelch 1.
REPEAT 290 338 Kelch 2.
REPEAT 346 399 Kelch 3.
REPEAT 402 453 Kelch 4.
REPEAT 459 511 Kelch 5.
REPEAT 525 575 Kelch 6.
DOMAIN 561 613 PSI 1.
DOMAIN 847 899 PSI 2.
DOMAIN 900 947 PSI 3.
DOMAIN 1074 1115 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1163 1210 Laminin EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 1211 1261 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 1263 1405 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1403 1445 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1522 1570 Kelch 7.
REPEAT 1580 1626 Kelch 8.
REPEAT 1632 1679 Kelch 9.
REPEAT 1685 1735 Kelch 10.
REPEAT 1796 1843 Kelch 11.
REPEAT 1852 1898 Kelch 12.
DOMAIN 1876 1916 PSI 4.
DOMAIN 1924 1979 PSI 5.
DOMAIN 2060 2118 PSI 6.
DOMAIN 2120 2177 PSI 7.
DOMAIN 2178 2216 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2253 2301 Laminin EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 2380 2443 Laminin EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
COMPBIAS 2528 2564 Pro-rich.
COMPBIAS 2739 2833 Gly-rich.
MOD_RES 1353 1353 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QYP0}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1048 1048 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1271 1271 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 2066 2066 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2229 2229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 57 {ECO:0000250}.
DISULFID 142 152 {ECO:0000250}.
DISULFID 146 158 {ECO:0000250}.
DISULFID 174 184 {ECO:0000250}.
DISULFID 178 191 {ECO:0000250}.
DISULFID 193 202 {ECO:0000250}.
DISULFID 1078 1091 {ECO:0000250}.
DISULFID 1085 1100 {ECO:0000250}.
DISULFID 1102 1114 {ECO:0000250}.
DISULFID 1163 1171 {ECO:0000250}.
DISULFID 1165 1179 {ECO:0000250}.
DISULFID 1182 1191 {ECO:0000250}.
DISULFID 1194 1208 {ECO:0000250}.
DISULFID 1211 1224 {ECO:0000250}.
DISULFID 1213 1231 {ECO:0000250}.
DISULFID 1233 1242 {ECO:0000250}.
DISULFID 1245 1259 {ECO:0000250}.
DISULFID 1263 1302 {ECO:0000250}.
DISULFID 1336 1367 {ECO:0000250}.
DISULFID 1407 1421 {ECO:0000250}.
DISULFID 1415 1433 {ECO:0000250}.
DISULFID 1435 1444 {ECO:0000250}.
DISULFID 2182 2195 {ECO:0000250}.
DISULFID 2189 2204 {ECO:0000250}.
DISULFID 2253 2261 {ECO:0000250}.
DISULFID 2255 2270 {ECO:0000250}.
DISULFID 2273 2282 {ECO:0000250}.
DISULFID 2285 2299 {ECO:0000250}.
DISULFID 2380 2389 {ECO:0000250}.
DISULFID 2382 2397 {ECO:0000250}.
DISULFID 2399 2424 {ECO:0000250}.
DISULFID 2427 2441 {ECO:0000250}.
VAR_SEQ 700 766 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9693030}.
/FTId=VSP_036067.
VARIANT 199 199 G -> R (in CRPT2).
{ECO:0000269|PubMed:23063620}.
/FTId=VAR_069305.
VARIANT 1566 1566 R -> H (in CRPT2; dbSNP:rs397515427).
{ECO:0000269|PubMed:23063620}.
/FTId=VAR_069306.
VARIANT 2434 2434 S -> G (in CRPT2; dbSNP:rs397515428).
{ECO:0000269|PubMed:23063620}.
/FTId=VAR_069307.
SEQUENCE 2845 AA; 303100 MW; DDBF0EE07511587D CRC64;
MALGKVLAMA LVLALAVLGS LSPGARAGDC KGQRQVLREA PGFVTDGAGN YSVNGNCEWL
IEAPSPQHRI LLDFLFLDTE CTYDYLFVYD GDSPRGPLLA SLSGSTRPPP IEASSGKMLL
HLFSDANYNL LGFNASFRFS LCPGGCQSHG QCQPPGVCAC EPGWGGPDCG LQECSAYCGS
HGTCASPLGP CRCEPGFLGR ACDLHLWENQ GAGWWHNVSA RDPAFSARIG AAGAFLSPPG
LLAVFGGQDL NNALGDLVLY NFSANTWESW DLSPAPAARH SHVAVAWAGS LVLMGGELAD
GSLTNDVWAF SPLGRGHWEL LAPPASSSSG PPGLAGHAAA LVDDVWLYVS GGRTPHDLFS
SGLFRFRLDS TSGGYWEQVI PAGGRPPAAT GHSMVFHAPS RALLVHGGHR PSTARFSVRV
NSTELFHVDR HVWTTLKGRD GLQGPRERAF HTASVLGNYM VVYGGNVHTH YQEEKCYEDG
IFFYHLGCHQ WVSGAELAPP GTPEGRAAPP SGRYSHVAAV LGGSVLLVAG GYSGRPRGDL
MAYKVPPFVF QAPAPDYHLD YCSMYTDHSV CSRDPECSWC QGACQAAPPP GTPLGACPAA
SCLGLGRLLG DCQACLAFSS PTAPPRGPGT LGWCVHNESC LPRPEQARCR GEQISGTVGW
WGPAPVFVTS LEACVTQSFL PGLHLLTFQQ PPNTSQPDKV SIVRSTTITL TPSAETDVSL
VYRGFIYPML PGGPGGPGAE DVAVWTRAQR LHVLARMARG PDTENMEEVG RWVAHQEKET
RRLQRPGSAR LFPLPGRDHK YAVEIQGQLN GSAGPGHSEL TLLWDRTGVP GGSEISFFFL
EPYRSSSCTS YSSCLGCLAD QGCGWCLTSA TCHLRQGGAH CGDDGAGGSL LVLVPTLCPL
CEEHRDCHAC TQDPFCEWHQ STSRKGDAAC SRRGRGRGAL KSPEECPPLC SQRLTCEDCL
ANSSQCAWCQ STHTCFLFAA YLARYPHGGC RGWDDSVHSE PRCRSCDGFL TCHECLQSHE
CGWCGNEDNP TLGRCLQGDF SGPLGGGNCS LWVGEGLGLP VALPARWAYA RCPDVDECRL
GLARCHPRAT CLNTPLSYEC HCQRGYQGDG ISHCNRTCLE DCGHGVCSGP PDFTCVCDLG
WTSDLPPPTP APGPPAPRCS RDCGCSFHSH CRKRGPGFCD ECQDWTWGEH CERCRPGSFG
NATGSRGCRP CQCNGHGDPR RGHCDNLSGL CFCQDHTEGA HCQLCSPGYY GDPRAGGSCF
RECGGRALLT NVSSVALGSR RVGGLLPPGG GAARAGPGLS YCVWVVSATE ELQPCAPGTL
CPPLTLTFSP DSSTPCTLSY VLAFDGFPRF LDTGVVQSDR SLIAAFCGQR RDRPLTVQAL
SGLLVLHWEA NGSSSWGFNA SVGSARCGSG GPGSCPVPQE CVPQDGAAGA GLCRCPQGWA
GPHCRMALCP ENCNAHTGAG TCNQSLGVCI CAEGFGGPDC ATKLDGGQLV WETLMDSRLS
ADTASRFLHR LGHTMVDGPD ATLWMFGGLG LPQGLLGNLY RYSVSERRWT QMLAGAEDGG
PGPSPRSFHA AAYVPAGRGA MYLLGGLTAG GVTRDFWVLN LTTLQWRQEK APQTVELPAV
AGHTLTARRG LSLLLVGGYS PENGFNQQLL EYQLATGTWV SGAQSGTPPT GLYGHSAVYH
EATDSLYVFG GFRFHVELAA PSPELYSLHC PDRTWSLLAP SQGAKRDRMR NVRGSSRGLG
QVPGEQPGSW GFREVRKKMA LWAALAGTGG FLEEISPHLK EPRPRLFHAS ALLGDTMVVL
GGRSDPDEFS SDVLLYQVNC NAWLLPDLTR SASVGPPMEE SVAHAVAAVG SRLYISGGFG
GVALGRLLAL TLPPDPCRLL SSPEACNQSG ACTWCHGACL SGDQAHRLGC GGSPCSPMPR
SPEECRRLRT CSECLARHPR TLQPGDGEAS TPRCKWCTNC PEGACIGRNG SCTSENDCRI
NQREVFWAGN CSEAACGAAD CEQCTREGKC MWTRQFKRTG ETRRILSVQP TYDWTCFSHS
LLNVSPMPVE SSPPLPCPTP CHLLPNCTSC LDSKGADGGW QHCVWSSSLQ QCLSPSYLPL
RCMAGGCGRL LRGPESCSLG CAQATQCALC LRRPHCGWCA WGGQDGGGRC MEGGLSGPRD
GLTCGRPGAS WAFLSCPPED ECANGHHDCN ETQNCHDQPH GYECSCKTGY TMDNMTGLCR
PVCAQGCVNG SCVEPDHCRC HFGFVGRNCS TECRCNRHSE CAGVGARDHC LLCRNHTKGS
HCEQCLPLFV GSAVGGGTCR PCHAFCRGNS HICISRKELQ MSKGEPKKYS LDPEEIENWV
TEGPSEDEAV CVNCQNNSYG EKCESCLQGY FLLDGKCTKC QCNGHADTCN EQDGTGCPCQ
NNTETGTCQG SSPSDRRDCY KYQCAKCRES FHGSPLGGQQ CYRLISVEQE CCLDPTSQTN
CFHEPKRRAL GPGRTVLFGV QPKFTNVDIR LTLDVTFGAV DLYVSTSYDT FVVRVAPDTG
VHTVHIQPPP APPPPPPPAD GGPRGAGDPG GAGASSGPGA PAEPRVREVW PRGLITYVTV
TEPSAVLVVR GVRDRLVITY PHEHHALKSS RFYLLLLGVG DPSGPGANGS ADSQGLLFFR
QDQAHIDLFV FFSVFFSCFF LFLSLCVLLW KAKQALDQRQ EQRRHLQEMT KMASRPFAKV
TVCFPPDPTA PASAWKPAGL PPPAFRRSEP FLAPLLLTGA GGPWGPMGGG CCPPAIPATT
AGLRAGPITL EPTEDGMAGV ATLLLQLPGG PHAPNGACLG SALVTLRHRL HEYCGGGGGA
GGSGHGTGAG RKGLLSQDNL TSMSL


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EIAAB14453 Fat2,Fath2,Megf1,Multiple EGF-like domains protein 1,Multiple epidermal growth factor-like domains protein 1,Protocadherin Fat 2,Rat,Rattus norvegicus
EIAAB06751 Cadherin EGF LAG seven-pass G-type receptor 3,Celsr3,Megf2,Multiple EGF-like domains protein 2,Multiple epidermal growth factor-like domains protein 2,Rat,Rattus norvegicus
EIAAB06748 Cadherin EGF LAG seven-pass G-type receptor 2,Celsr2,Megf3,Multiple EGF-like domains protein 3,Multiple epidermal growth factor-like domains protein 3,Rat,Rattus norvegicus
EIAAB30505 Homo sapiens,hPEAR1,Human,MEGF12,Multiple EGF-like domains protein 12,Multiple epidermal growth factor-like domains protein 12,PEAR1,Platelet endothelial aggregation receptor 1
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
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
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
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
E0589Rb Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 11 96T
TRI25_HUMAN Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 6 96T
E0589h 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
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
CSB-EL013680RA Rat Multiple epidermal growth factor-like domains protein 6(MEGF6) ELISA kit 96T
E15038h Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 10 96T
CSB-EL013680MO Mouse Multiple epidermal growth factor-like domains protein 6(MEGF6) ELISA kit 96T
CSB-EL013681MO Mouse Multiple epidermal growth factor-like domains protein 8(MEGF8) ELISA kit 96T


 

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