Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Slit homolog 1 protein (Slit-1) (Multiple epidermal growth factor-like domains protein 4) (Multiple EGF-like domains protein 4)

 SLIT1_HUMAN             Reviewed;        1534 AA.
O75093; Q5T0V1; Q8WWZ2; Q9UIL7;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 4.
18-JUL-2018, entry version 173.
RecName: Full=Slit homolog 1 protein;
Short=Slit-1;
AltName: Full=Multiple epidermal growth factor-like domains protein 4;
Short=Multiple EGF-like domains protein 4;
Flags: Precursor;
Name=SLIT1; Synonyms=KIAA0813, MEGF4, SLIL1;
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 1), AND TISSUE SPECIFICITY.
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).
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.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
SEQUENCE REVISION.
Nakayama M., Nakajima D., Ohara O.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-1534 (ISOFORM 2).
PubMed=12141424;
Little M., Rumballe B., Georgas K., Yamada T., Teasdale R.D.;
"Conserved modularity and potential for alternate splicing in mouse
and human Slit genes.";
Int. J. Dev. Biol. 46:385-391(2002).
[9]
REVIEW.
PubMed=12200164; DOI=10.1016/S0959-437X(02)00343-X;
Wong K., Park H.T., Wu J.Y., Rao Y.;
"Slit proteins: molecular guidance cues for cells ranging from neurons
to leukocytes.";
Curr. Opin. Genet. Dev. 12:583-591(2002).
-!- FUNCTION: Thought to act as molecular guidance cue in cellular
migration, and function appears to be mediated by interaction with
roundabout homolog receptors. During neural development involved
in axonal navigation at the ventral midline of the neural tube and
projection of axons to different regions (By similarity). SLIT1
and SLIT2 together seem to be essential for midline guidance in
the forebrain by acting as repulsive signal preventing
inappropriate midline crossing by axons projecting from the
olfactory bulb. {ECO:0000250}.
-!- SUBUNIT: Interacts with ROBO1 and GREM1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75093-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=O75093-2; Sequence=VSP_009706, VSP_009707, VSP_009708;
-!- TISSUE SPECIFICITY: Predominantly expressed in adult forebrain.
Expressed in fetal brain, lung and kidney.
{ECO:0000269|PubMed:9813312}.
-!- SEQUENCE CAUTION:
Sequence=BAA32465.3; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB017167; BAA35184.1; -; mRNA.
EMBL; AB011537; BAA32465.3; ALT_INIT; mRNA.
EMBL; AL442123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49958.1; -; Genomic_DNA.
EMBL; BC146851; AAI46852.1; -; mRNA.
EMBL; AY029183; AAK31796.1; -; mRNA.
CCDS; CCDS7453.1; -. [O75093-1]
RefSeq; NP_003052.2; NM_003061.2. [O75093-1]
UniGene; Hs.632082; -.
ProteinModelPortal; O75093; -.
BioGrid; 112472; 2.
IntAct; O75093; 16.
STRING; 9606.ENSP00000266058; -.
CarbonylDB; O75093; -.
iPTMnet; O75093; -.
PhosphoSitePlus; O75093; -.
BioMuta; SLIT1; -.
EPD; O75093; -.
PaxDb; O75093; -.
PeptideAtlas; O75093; -.
PRIDE; O75093; -.
ProteomicsDB; 49753; -.
ProteomicsDB; 49754; -. [O75093-2]
Ensembl; ENST00000266058; ENSP00000266058; ENSG00000187122. [O75093-1]
GeneID; 6585; -.
KEGG; hsa:6585; -.
UCSC; uc001kmw.3; human. [O75093-1]
CTD; 6585; -.
DisGeNET; 6585; -.
EuPathDB; HostDB:ENSG00000187122.16; -.
GeneCards; SLIT1; -.
H-InvDB; HIX0079168; -.
H-InvDB; HIX0170440; -.
HGNC; HGNC:11085; SLIT1.
HPA; HPA006879; -.
MIM; 603742; gene.
neXtProt; NX_O75093; -.
OpenTargets; ENSG00000187122; -.
PharmGKB; PA35938; -.
eggNOG; KOG4237; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00910000144018; -.
HOGENOM; HOG000116120; -.
HOVERGEN; HBG057959; -.
InParanoid; O75093; -.
KO; K06838; -.
OrthoDB; EOG091G0MHP; -.
PhylomeDB; O75093; -.
TreeFam; TF332887; -.
Reactome; R-HSA-373752; Netrin-1 signaling.
Reactome; R-HSA-376176; Signaling by ROBO receptors.
Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
Reactome; R-HSA-8985801; Regulation of cortical dendrite branching.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
SIGNOR; O75093; -.
ChiTaRS; SLIT1; human.
GeneWiki; SLIT1; -.
GenomeRNAi; 6585; -.
PRO; PR:O75093; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000187122; -.
CleanEx; HS_SLIT1; -.
ExpressionAtlas; O75093; baseline and differential.
Genevisible; O75093; HS.
GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
GO; GO:0033563; P:dorsal/ventral axon guidance; IEA:Ensembl.
GO; GO:0048853; P:forebrain morphogenesis; NAS:UniProtKB.
GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
Gene3D; 3.80.10.10; -; 5.
InterPro; IPR013320; ConA-like_dom_sf.
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; IPR003645; Fol_N.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001791; Laminin_G.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF00008; EGF; 5.
Pfam; PF12661; hEGF; 2.
Pfam; PF02210; Laminin_G_2; 1.
Pfam; PF13855; LRR_8; 6.
Pfam; PF01463; LRRCT; 4.
Pfam; PF01462; LRRNT; 4.
SMART; SM00041; CT; 1.
SMART; SM00181; EGF; 9.
SMART; SM00179; EGF_CA; 7.
SMART; SM00274; FOLN; 4.
SMART; SM00282; LamG; 1.
SMART; SM00369; LRR_TYP; 18.
SMART; SM00082; LRRCT; 4.
SMART; SM00013; LRRNT; 4.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS01185; CTCK_1; 1.
PROSITE; PS01225; CTCK_2; 1.
PROSITE; PS00022; EGF_1; 9.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 9.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS50025; LAM_G_DOMAIN; 1.
PROSITE; PS51450; LRR; 21.
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 1534 Slit homolog 1 protein.
/FTId=PRO_0000007722.
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 273 309 LRRNT 2.
REPEAT 310 331 LRR 7.
REPEAT 334 355 LRR 8.
REPEAT 358 379 LRR 9.
REPEAT 382 403 LRR 10.
REPEAT 406 427 LRR 11.
DOMAIN 439 489 LRRCT 2.
DOMAIN 504 540 LRRNT 3.
REPEAT 541 562 LRR 12.
REPEAT 566 587 LRR 13.
REPEAT 590 611 LRR 14.
REPEAT 614 635 LRR 15.
REPEAT 638 659 LRR 16.
DOMAIN 671 721 LRRCT 3.
DOMAIN 725 761 LRRNT 4.
REPEAT 762 783 LRR 17.
REPEAT 785 806 LRR 18.
REPEAT 809 830 LRR 19.
REPEAT 833 854 LRR 20.
DOMAIN 866 916 LRRCT 4.
DOMAIN 927 962 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 964 1003 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1005 1041 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1043 1081 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1083 1119 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1127 1163 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1166 1339 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1340 1374 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1377 1413 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1418 1454 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1459 1534 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 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 630 630 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 762 762 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 801 801 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 806 806 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1026 1026 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1079 1079 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1189 1189 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1259 1259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1306 1306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 286 295 {ECO:0000250}.
DISULFID 443 466 {ECO:0000250}.
DISULFID 445 487 {ECO:0000250}.
DISULFID 513 519 {ECO:0000250}.
DISULFID 517 526 {ECO:0000250}.
DISULFID 675 698 {ECO:0000250}.
DISULFID 677 719 {ECO:0000250}.
DISULFID 929 940 {ECO:0000250}.
DISULFID 934 950 {ECO:0000250}.
DISULFID 952 961 {ECO:0000250}.
DISULFID 968 979 {ECO:0000250}.
DISULFID 973 991 {ECO:0000250}.
DISULFID 993 1002 {ECO:0000250}.
DISULFID 1009 1020 {ECO:0000250}.
DISULFID 1014 1029 {ECO:0000250}.
DISULFID 1031 1040 {ECO:0000250}.
DISULFID 1047 1060 {ECO:0000250}.
DISULFID 1054 1069 {ECO:0000250}.
DISULFID 1071 1080 {ECO:0000250}.
DISULFID 1087 1098 {ECO:0000250}.
DISULFID 1092 1107 {ECO:0000250}.
DISULFID 1109 1118 {ECO:0000250}.
DISULFID 1131 1142 {ECO:0000250}.
DISULFID 1136 1151 {ECO:0000250}.
DISULFID 1153 1162 {ECO:0000250}.
DISULFID 1313 1339 {ECO:0000250}.
DISULFID 1342 1352 {ECO:0000250}.
DISULFID 1347 1362 {ECO:0000250}.
DISULFID 1364 1373 {ECO:0000250}.
DISULFID 1381 1391 {ECO:0000250}.
DISULFID 1386 1401 {ECO:0000250}.
DISULFID 1403 1412 {ECO:0000250}.
DISULFID 1422 1432 {ECO:0000250}.
DISULFID 1427 1442 {ECO:0000250}.
DISULFID 1444 1453 {ECO:0000250}.
DISULFID 1459 1498 {ECO:0000250}.
DISULFID 1477 1512 {ECO:0000250}.
DISULFID 1488 1528 {ECO:0000250}.
DISULFID 1492 1530 {ECO:0000250}.
VAR_SEQ 338 338 I -> IRPLSFCSPCR (in isoform 2).
{ECO:0000303|PubMed:12141424}.
/FTId=VSP_009706.
VAR_SEQ 790 813 Missing (in isoform 2).
{ECO:0000303|PubMed:12141424}.
/FTId=VSP_009707.
VAR_SEQ 830 1534 Missing (in isoform 2).
{ECO:0000303|PubMed:12141424}.
/FTId=VSP_009708.
VARIANT 824 824 P -> L (in dbSNP:rs2817673).
/FTId=VAR_049003.
CONFLICT 99 99 A -> V (in Ref. 2; BAA32465).
{ECO:0000305}.
CONFLICT 163 163 Q -> R (in Ref. 1; BAA35184).
{ECO:0000305}.
CONFLICT 829 829 Q -> P (in Ref. 8; AAK31796).
{ECO:0000305}.
CONFLICT 966 966 D -> N (in Ref. 1; BAA35184).
{ECO:0000305}.
SEQUENCE 1534 AA; 167926 MW; 47B11CE6704A3E1D CRC64;
MALTPGWGSS AGPVRPELWL LLWAAAWRLG ASACPALCTC TGTTVDCHGT GLQAIPKNIP
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ
LHMLPELLFQ NNQALSRLDL SENAIQAIPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT
QCSGPASLRG LNVAEVQKSE FSCSGQGEAG RVPTCTLSSG SCPAMCTCSN GIVDCRGKGL
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TSGARCASPR RLANKRIGQI
KSKKFRCSAK EQYFIPGTED YQLNSECNSD VVCPHKCRCE ANVVECSSLK LTKIPERIPQ
STAELRLNNN EISILEATGM FKKLTHLKKI NLSNNKVSEI EDGAFEGAAS VSELHLTANQ
LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNQIT TVSPGAFDTL
QSLSTLNLLA NPFNCNCQLA WLGGWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE
EGQEEGGCLP RPQCPQECAC LDTVVRCSNK HLRALPKGIP KNVTELYLDG NQFTLVPGQL
STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH
GNDISTLQEG IFADVTSLSH LAIGANPLYC DCHLRWLSSW VKTGYKEPGI ARCAGPQDME
GKLLLTTPAK KFECQGPPTL AVQAKCDLCL SSPCQNQGTC HNDPLEVYRC ACPSGYKGRD
CEVSLDSCSS GPCENGGTCH AQEGEDAPFT CSCPTGFEGP TCGVNTDDCV DHACANGGVC
VDGVGNYTCQ CPLQYEGKAC EQLVDLCSPD LNPCQHEAQC VGTPDGPRCE CMPGYAGDNC
SENQDDCRDH RCQNGAQCMD EVNSYSCLCA EGYSGQLCEI PPHLPAPKSP CEGTECQNGA
NCVDQGNRPV CQCLPGFGGP ECEKLLSVNF VDRDTYLQFT DLQNWPRANI TLQVSTAEDN
GILLYNGDND HIAVELYQGH VRVSYDPGSY PSSAIYSAET INDGQFHTVE LVAFDQMVNL
SIDGGSPMTM DNFGKHYTLN SEAPLYVGGM PVDVNSAAFR LWQILNGTGF HGCIRNLYIN
NELQDFTKTQ MKPGVVPGCE PCRKLYCLHG ICQPNATPGP MCHCEAGWVG LHCDQPADGP
CHGHKCVHGQ CVPLDALSYS CQCQDGYSGA LCNQAGALAE PCRGLQCLHG HCQASGTKGA
HCVCDPGFSG ELCEQESECR GDPVRDFHQV QRGYAICQTT RPLSWVECRG SCPGQGCCQG
LRLKRRKFTF ECSDGTSFAE EVEKPTKCGC ALCA


Related products :

Catalog number Product name Quantity
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
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur