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Slit homolog 3 protein (Slit-3) (Multiple epidermal growth factor-like domains protein 5) (Multiple EGF-like domains protein 5)

 SLIT3_HUMAN             Reviewed;        1523 AA.
O75094; A6H8U9; J3KNP3; O95804; Q9UFH5;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
27-SEP-2017, entry version 162.
RecName: Full=Slit homolog 3 protein;
Short=Slit-3;
AltName: Full=Multiple epidermal growth factor-like domains protein 5;
Short=Multiple EGF-like domains protein 5;
Flags: Precursor;
Name=SLIT3; Synonyms=KIAA0814, MEGF5, SLIL2; ORFNames=UNQ691/PRO1336;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
AND VARIANT ALA-371.
PubMed=9813312; DOI=10.1016/S0169-328X(98)00224-1;
Itoh A., Miyabayashi T., Ohno M., Sakano S.;
"Cloning and expressions of three mammalian homologues of Drosophila
slit suggest possible roles for Slit in the formation and maintenance
of the nervous system.";
Brain Res. Mol. Brain Res. 62:175-186(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-371.
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).
[3]
SEQUENCE REVISION.
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-371 AND SER-618.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-371.
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-657, AND VARIANT
ALA-371.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 574-1523 (ISOFORM 2).
PubMed=10349621; DOI=10.1016/S0925-4773(98)00174-9;
Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T.,
Little M.H.;
"Distinct but overlapping expression patterns of two vertebrate slit
homologs implies functional roles in CNS development and
organogenesis.";
Mech. Dev. 79:57-72(1998).
-!- FUNCTION: May act as molecular guidance cue in cellular migration,
and function may be mediated by interaction with roundabout
homolog receptors.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O75094-1; Sequence=Displayed;
Name=2;
IsoId=O75094-2; Sequence=VSP_009714;
Name=3;
IsoId=O75094-3; Sequence=VSP_009715;
Name=4;
IsoId=O75094-4; Sequence=VSP_054798;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in thyroid.
{ECO:0000269|PubMed:9813312}.
-!- SEQUENCE CAUTION:
Sequence=BAA32466.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB59249.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SLIT3ID50515ch5q34.html";
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EMBL; AB017169; BAA35186.1; -; mRNA.
EMBL; AB011538; BAA32466.2; ALT_INIT; mRNA.
EMBL; AY358884; AAQ89243.1; -; mRNA.
EMBL; AC008409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC027311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC094081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC146759; AAI46760.1; -; mRNA.
EMBL; AL122074; CAB59249.1; ALT_SEQ; mRNA.
EMBL; AF075240; AAD19336.1; -; mRNA.
CCDS; CCDS4369.1; -. [O75094-1]
CCDS; CCDS64311.1; -. [O75094-4]
PIR; T34555; T34555.
RefSeq; NP_001258875.1; NM_001271946.1.
RefSeq; NP_003053.1; NM_003062.3.
UniGene; Hs.552087; -.
ProteinModelPortal; O75094; -.
BioGrid; 112473; 2.
IntAct; O75094; 4.
MINT; MINT-2797284; -.
STRING; 9606.ENSP00000430333; -.
iPTMnet; O75094; -.
PhosphoSitePlus; O75094; -.
MaxQB; O75094; -.
PaxDb; O75094; -.
PeptideAtlas; O75094; -.
PRIDE; O75094; -.
Ensembl; ENST00000332966; ENSP00000332164; ENSG00000184347. [O75094-4]
Ensembl; ENST00000519560; ENSP00000430333; ENSG00000184347. [O75094-1]
GeneID; 6586; -.
KEGG; hsa:6586; -.
UCSC; uc003mab.5; human. [O75094-1]
CTD; 6586; -.
DisGeNET; 6586; -.
EuPathDB; HostDB:ENSG00000184347.14; -.
GeneCards; SLIT3; -.
H-InvDB; HIX0005394; -.
HGNC; HGNC:11087; SLIT3.
HPA; HPA051630; -.
MIM; 603745; gene.
neXtProt; NX_O75094; -.
OpenTargets; ENSG00000184347; -.
PharmGKB; PA35940; -.
eggNOG; KOG4237; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00880000137863; -.
HOGENOM; HOG000116120; -.
HOVERGEN; HBG057959; -.
InParanoid; O75094; -.
KO; K06850; -.
OMA; CQLSPRC; -.
OrthoDB; EOG091G0MHP; -.
PhylomeDB; O75094; -.
TreeFam; TF332887; -.
Reactome; R-HSA-373752; Netrin-1 signaling.
ChiTaRS; SLIT3; human.
GeneWiki; SLIT3; -.
GenomeRNAi; 6586; -.
PRO; PR:O75094; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000184347; -.
CleanEx; HS_SLIT3; -.
ExpressionAtlas; O75094; baseline and differential.
Genevisible; O75094; HS.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB.
GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0051414; P:response to cortisol; IEP:UniProtKB.
GO; GO:0035385; P:Roundabout signaling pathway; IMP:BHF-UCL.
Gene3D; 3.80.10.10; -; 6.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR006207; Cys_knot_C.
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_.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001791; Laminin_G.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR000372; LRRNT.
Pfam; PF00008; EGF; 6.
Pfam; PF02210; Laminin_G_2; 1.
Pfam; PF13855; LRR_8; 5.
Pfam; PF01463; LRRCT; 4.
Pfam; PF01462; LRRNT; 3.
SMART; SM00041; CT; 1.
SMART; SM00181; EGF; 9.
SMART; SM00179; EGF_CA; 9.
SMART; SM00282; LamG; 1.
SMART; SM00369; LRR_TYP; 18.
SMART; SM00082; LRRCT; 4.
SMART; SM00013; LRRNT; 4.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF52058; SSF52058; 4.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS01185; CTCK_1; 1.
PROSITE; PS01225; CTCK_2; 1.
PROSITE; PS00022; EGF_1; 9.
PROSITE; PS01186; EGF_2; 7.
PROSITE; PS50026; EGF_3; 9.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS50025; LAM_G_DOMAIN; 1.
PROSITE; PS51450; LRR; 20.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
Leucine-rich repeat; Neurogenesis; Polymorphism; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 1523 Slit homolog 3 protein.
/FTId=PRO_0000007732.
DOMAIN 34 61 LRRNT.
REPEAT 62 83 LRR 1.
REPEAT 86 107 LRR 2.
REPEAT 110 131 LRR 3.
REPEAT 134 155 LRR 4.
REPEAT 158 179 LRR 5.
REPEAT 182 203 LRR 6.
DOMAIN 215 265 LRRCT 1.
DOMAIN 271 307 LRRNT 2.
REPEAT 308 329 LRR 7.
REPEAT 332 353 LRR 8.
REPEAT 356 377 LRR 9.
REPEAT 380 401 LRR 10.
REPEAT 404 425 LRR 11.
DOMAIN 437 487 LRRCT 2.
DOMAIN 496 532 LRRNT 3.
REPEAT 533 554 LRR 12.
REPEAT 558 579 LRR 13.
REPEAT 582 603 LRR 14.
REPEAT 606 627 LRR 15.
REPEAT 630 651 LRR 16.
DOMAIN 663 713 LRRCT 3.
DOMAIN 716 752 LRRNT 4.
REPEAT 753 775 LRR 17.
REPEAT 776 797 LRR 18.
REPEAT 800 821 LRR 19.
REPEAT 824 845 LRR 20.
DOMAIN 857 907 LRRCT 4.
DOMAIN 918 953 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 955 994 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 996 1032 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1034 1072 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1074 1110 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1119 1155 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1158 1332 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1340 1365 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1368 1403 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1408 1444 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1449 1523 CTCK. {ECO:0000255|PROSITE-
ProRule:PRU00039}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 784 784 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 792 792 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 797 797 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 928 928 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1008 1008 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1025 1025 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1181 1181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1247 1247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1406 1406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 284 293 {ECO:0000250}.
DISULFID 441 464 {ECO:0000250}.
DISULFID 443 485 {ECO:0000250}.
DISULFID 505 511 {ECO:0000250}.
DISULFID 509 518 {ECO:0000250}.
DISULFID 667 690 {ECO:0000250}.
DISULFID 669 711 {ECO:0000250}.
DISULFID 920 931 {ECO:0000250}.
DISULFID 925 941 {ECO:0000250}.
DISULFID 943 952 {ECO:0000250}.
DISULFID 959 970 {ECO:0000250}.
DISULFID 964 982 {ECO:0000250}.
DISULFID 984 993 {ECO:0000250}.
DISULFID 1000 1011 {ECO:0000250}.
DISULFID 1005 1020 {ECO:0000250}.
DISULFID 1022 1031 {ECO:0000250}.
DISULFID 1038 1051 {ECO:0000250}.
DISULFID 1045 1060 {ECO:0000250}.
DISULFID 1062 1071 {ECO:0000250}.
DISULFID 1078 1089 {ECO:0000250}.
DISULFID 1083 1098 {ECO:0000250}.
DISULFID 1100 1109 {ECO:0000250}.
DISULFID 1123 1134 {ECO:0000250}.
DISULFID 1128 1143 {ECO:0000250}.
DISULFID 1145 1154 {ECO:0000250}.
DISULFID 1305 1332 {ECO:0000250}.
DISULFID 1355 1364 {ECO:0000250}.
DISULFID 1372 1382 {ECO:0000250}.
DISULFID 1377 1391 {ECO:0000250}.
DISULFID 1393 1402 {ECO:0000250}.
DISULFID 1412 1422 {ECO:0000250}.
DISULFID 1417 1432 {ECO:0000250}.
DISULFID 1434 1443 {ECO:0000250}.
DISULFID 1449 1487 {ECO:0000250}.
DISULFID 1467 1501 {ECO:0000250}.
DISULFID 1478 1517 {ECO:0000250}.
DISULFID 1482 1519 {ECO:0000250}.
VAR_SEQ 906 906 K -> KVLWFCCP (in isoform 4).
{ECO:0000305}.
/FTId=VSP_054798.
VAR_SEQ 1117 1216 Missing (in isoform 2).
{ECO:0000303|PubMed:10349621,
ECO:0000303|PubMed:9813312}.
/FTId=VSP_009714.
VAR_SEQ 1446 1523 ENPCLGQVVREVIRRQKGYASCATASKVPIMECRGGCGPQC
CQPTRSKRRKYVFQCTDGSSFVEEVERHLECGCLACS ->
VFRAQVFQSSLPGNCSWSCWPPRPPMP (in isoform
3). {ECO:0000303|PubMed:9813312}.
/FTId=VSP_009715.
VARIANT 371 371 V -> A (in dbSNP:rs891921).
{ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:9693030,
ECO:0000269|PubMed:9813312}.
/FTId=VAR_049004.
VARIANT 395 395 R -> Q (in dbSNP:rs2288792).
/FTId=VAR_021905.
VARIANT 618 618 G -> S (in dbSNP:rs10036727).
{ECO:0000269|PubMed:12975309}.
/FTId=VAR_024265.
VARIANT 810 810 R -> Q (in dbSNP:rs36052924).
/FTId=VAR_049005.
VARIANT 994 994 E -> G (in dbSNP:rs2305993).
/FTId=VAR_020168.
VARIANT 1064 1064 P -> A (in dbSNP:rs10072243).
/FTId=VAR_049006.
SEQUENCE 1523 AA; 167713 MW; CEB00887F6908554 CRC64;
MAPGWAGVGA AVRARLALAL ALASVLSGPP AVACPTKCTC SAASVDCHGL GLRAVPRGIP
RNAERLDLDR NNITRITKMD FAGLKNLRVL HLEDNQVSVI ERGAFQDLKQ LERLRLNKNK
LQVLPELLFQ STPKLTRLDL SENQIQGIPR KAFRGITDVK NLQLDNNHIS CIEDGAFRAL
RDLEILTLNN NNISRILVTS FNHMPKIRTL RLHSNHLYCD CHLAWLSDWL RQRRTVGQFT
LCMAPVHLRG FNVADVQKKE YVCPAPHSEP PSCNANSISC PSPCTCSNNI VDCRGKGLME
IPANLPEGIV EIRLEQNSIK AIPAGAFTQY KKLKRIDISK NQISDIAPDA FQGLKSLTSL
VLYGNKITEI VKGLFDGLVS LQLLLLNANK INCLRVNTFQ DLQNLNLLSL YDNKLQTISK
GLFAPLQSIQ TLHLAQNPFV CDCHLKWLAD YLQDNPIETS GARCSSPRRL ANKRISQIKS
KKFRCSGSED YRSRFSSECF MDLVCPEKCR CEGTIVDCSN QKLVRIPSHL PEYVTDLRLN
DNEVSVLEAT GIFKKLPNLR KINLSNNKIK EVREGAFDGA ASVQELMLTG NQLETVHGRV
FRGLSGLKTL MLRSNLIGCV SNDTFAGLSS VRLLSLYDNR ITTITPGAFT TLVSLSTINL
LSNPFNCNCH LAWLGKWLRK RRIVSGNPRC QKPFFLKEIP IQDVAIQDFT CDGNEESSCQ
LSPRCPEQCT CMETVVRCSN KGLRALPRGM PKDVTELYLE GNHLTAVPRE LSALRHLTLI
DLSNNSISML TNYTFSNMSH LSTLILSYNR LRCIPVHAFN GLRSLRVLTL HGNDISSVPE
GSFNDLTSLS HLALGTNPLH CDCSLRWLSE WVKAGYKEPG IARCSSPEPM ADRLLLTTPT
HRFQCKGPVD INIVAKCNAC LSSPCKNNGT CTQDPVELYR CACPYSYKGK DCTVPINTCI
QNPCQHGGTC HLSDSHKDGF SCSCPLGFEG QRCEINPDDC EDNDCENNAT CVDGINNYVC
ICPPNYTGEL CDEVIDHCVP ELNLCQHEAK CIPLDKGFSC ECVPGYSGKL CETDNDDCVA
HKCRHGAQCV DTINGYTCTC PQGFSGPFCE HPPPMVLLQT SPCDQYECQN GAQCIVVQQE
PTCRCPPGFA GPRCEKLITV NFVGKDSYVE LASAKVRPQA NISLQVATDK DNGILLYKGD
NDPLALELYQ GHVRLVYDSL SSPPTTVYSV ETVNDGQFHS VELVTLNQTL NLVVDKGTPK
SLGKLQKQPA VGINSPLYLG GIPTSTGLSA LRQGTDRPLG GFHGCIHEVR INNELQDFKA
LPPQSLGVSP GCKSCTVCKH GLCRSVEKDS VVCECRPGWT GPLCDQEARD PCLGHRCHHG
KCVATGTSYM CKCAEGYGGD LCDNKNDSAN ACSAFKCHHG QCHISDQGEP YCLCQPGFSG
EHCQQENPCL GQVVREVIRR QKGYASCATA SKVPIMECRG GCGPQCCQPT RSKRRKYVFQ
CTDGSSFVEE VERHLECGCL ACS


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EIAAB12605 EGFL7,EGF-like protein 7,Epidermal growth factor-like protein 7,Homo sapiens,Human,MEGF7,Multiple EGF-like domains protein 7,Multiple epidermal growth factor-like domains protein 7,NOTCH4-like protein
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
EIAAB30506 Jagged and Delta protein,Jedi,Megf12,Mouse,mPEAR1,Multiple EGF-like domains protein 12,Multiple epidermal growth factor-like domains protein 12,Mus musculus,Pear1,Platelet endothelial aggregation rece
EIAAB12604 Cbl20,Egfl7,EGF-like protein 7,Epidermal growth factor-like protein 7,Megf7,Multiple EGF-like domains protein 7,Multiple epidermal growth factor-like domains protein 7,Rat,Rattus norvegicus
EIAAB14453 Fat2,Fath2,Megf1,Multiple EGF-like domains protein 1,Multiple epidermal growth factor-like domains protein 1,Protocadherin Fat 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
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
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
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
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-EL013680RA Rat Multiple epidermal growth factor-like domains protein 6(MEGF6) ELISA kit 96T
TRI25_HUMAN Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 6 96T
CSB-EL013681RA Rat Multiple epidermal growth factor-like domains protein 8(MEGF8) ELISA kit 96T
E0589Rb Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 11 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


 

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