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_RAT               Reviewed;        1531 AA.
O88279; Q8CJG8; Q8CJG9; Q8CJH0; Q9QWL1; Q9WUG5;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 148.
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=Megf4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; 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]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10102268; DOI=10.1016/S0092-8674(00)80590-5;
Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S.,
Tessier-Lavigne M., Kidd T.;
"Slit proteins bind Robo receptors and have an evolutionarily
conserved role in repulsive axon guidance.";
Cell 96:795-806(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
STRAIN=Sprague-Dawley; TISSUE=Brain;
Tanno T.;
"Alternative splicing for slit-1 in rat brain.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1209-1404 (ISOFORMS 1/2/3/4), 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).
[5]
FUNCTION.
PubMed=10864956;
Ringstedt T., Braisted J.E., Brose K., Kidd T., Goodman C.,
Tessier-Lavigne M., O'Leary D.D.;
"Slit inhibition of retinal axon growth and its role in retinal axon
pathfinding and innervation patterns in the diencephalon.";
J. Neurosci. 20:4983-4991(2000).
[6]
DEVELOPMENTAL STAGE.
PubMed=11754167; DOI=10.1002/cne.10068;
Marillat V., Cases O., Nguyen-Ba-Charvet K.T., Tessier-Lavigne M.,
Sotelo C., Chedotal A.;
"Spatiotemporal expression patterns of slit and robo genes in the rat
brain.";
J. Comp. Neurol. 442:130-155(2002).
[7]
INTERACTION WITH GREM1.
PubMed=15528323; DOI=10.4049/jimmunol.173.10.5914;
Chen B., Blair D.G., Plisov S., Vasiliev G., Perantoni A.O., Chen Q.,
Athanasiou M., Wu J.Y., Oppenheim J.J., Yang D.;
"Bone morphogenetic protein antagonists Drm/Gremlin and Dan interact
with Slits and act as negative regulators of monocyte chemotaxis.";
J. Immunol. 173:5914-5917(2004).
-!- 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. 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 (By
similarity). {ECO:0000250, ECO:0000269|PubMed:10864956}.
-!- SUBUNIT: Interacts with ROBO1 (By similarity) and GREM1.
{ECO:0000250, ECO:0000269|PubMed:15528323}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O88279-1; Sequence=Displayed;
Name=2; Synonyms=Sb;
IsoId=O88279-2; Sequence=VSP_009710, VSP_009711;
Name=3; Synonyms=La;
IsoId=O88279-3; Sequence=VSP_009712, VSP_009713;
Name=4; Synonyms=Sa;
IsoId=O88279-4; Sequence=VSP_009709;
-!- TISSUE SPECIFICITY: In adult brains expressed in the hippocampus,
cerebral cortex, and olfactory bulb but not in the cerebellum. In
embryo expressed in cerebral cortex. {ECO:0000269|PubMed:9813312}.
-!- DEVELOPMENTAL STAGE: Detected between E15 and E20, between P0 and
P10, and in adult in different regions of the telencephalon and
diencephalon. {ECO:0000269|PubMed:11754167}.
-!- SEQUENCE CAUTION:
Sequence=BAC21664.1; 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; AB011530; BAA32460.1; -; mRNA.
EMBL; AF133730; AAD25540.1; -; mRNA.
EMBL; AB073213; BAC21664.1; ALT_INIT; mRNA.
EMBL; AB073214; BAC21665.1; -; mRNA.
EMBL; AB073215; BAC21666.1; -; mRNA.
EMBL; AB017170; BAA35187.1; -; mRNA.
PIR; T42218; T42218.
RefSeq; NP_075242.1; NM_022953.2. [O88279-1]
UniGene; Rn.30002; -.
ProteinModelPortal; O88279; -.
STRING; 10116.ENSRNOP00000035315; -.
iPTMnet; O88279; -.
PhosphoSitePlus; O88279; -.
PaxDb; O88279; -.
PRIDE; O88279; -.
GeneID; 65047; -.
KEGG; rno:65047; -.
UCSC; RGD:69307; rat. [O88279-1]
CTD; 6585; -.
RGD; 69307; Slit1.
eggNOG; KOG4237; Eukaryota.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000116120; -.
HOVERGEN; HBG057959; -.
InParanoid; O88279; -.
KO; K06838; -.
PhylomeDB; O88279; -.
PRO; PR:O88279; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IDA:RGD.
GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
GO; GO:0021510; P:spinal cord development; IEP:RGD.
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; 4.
Pfam; PF12661; hEGF; 3.
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; 3.
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; 20.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
Leucine-rich repeat; Neurogenesis; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 1531 Slit homolog 1 protein.
/FTId=PRO_0000007724.
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 1124 1160 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1163 1336 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1337 1371 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1374 1410 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1415 1451 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1456 1531 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 1186 1186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1256 1256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1303 1303 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 1128 1139 {ECO:0000250}.
DISULFID 1133 1148 {ECO:0000250}.
DISULFID 1150 1159 {ECO:0000250}.
DISULFID 1310 1336 {ECO:0000250}.
DISULFID 1339 1349 {ECO:0000250}.
DISULFID 1344 1359 {ECO:0000250}.
DISULFID 1361 1370 {ECO:0000250}.
DISULFID 1378 1388 {ECO:0000250}.
DISULFID 1383 1398 {ECO:0000250}.
DISULFID 1400 1409 {ECO:0000250}.
DISULFID 1419 1429 {ECO:0000250}.
DISULFID 1424 1439 {ECO:0000250}.
DISULFID 1441 1450 {ECO:0000250}.
DISULFID 1456 1495 {ECO:0000250}.
DISULFID 1474 1509 {ECO:0000250}.
DISULFID 1485 1525 {ECO:0000250}.
DISULFID 1489 1527 {ECO:0000250}.
VAR_SEQ 113 136 Missing (in isoform 4).
{ECO:0000303|Ref.3}.
/FTId=VSP_009709.
VAR_SEQ 1412 1474 VGAVAEPCGGLQCLHGHCQASATRGAHCVCSPGFSGELCEQ
ESECRGDPVRDFHRVQRGYAIC -> SPSAGGTLSGTFTGS
RGAMPSARPRAHCHGWNAGARARARAAARAAAEAEEAHLRV
QRWDLVC (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_009710.
VAR_SEQ 1453 1458 ESECRG -> GQGAPS (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_009712.
VAR_SEQ 1459 1531 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_009713.
VAR_SEQ 1475 1531 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_009711.
CONFLICT 75 75 R -> W (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 96 96 Q -> P (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 100 100 V -> A (in Ref. 3; BAC21666).
{ECO:0000305}.
CONFLICT 102 102 R -> P (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 108 108 M -> V (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 113 115 RLR -> PFQ (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 123 123 V -> M (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 171 171 C -> R (in Ref. 3; BAC21664).
{ECO:0000305}.
CONFLICT 264 264 S -> T (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 408 408 S -> P (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 442 443 IC -> TW (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 468 468 S -> T (in Ref. 3; BAC21666).
{ECO:0000305}.
CONFLICT 523 523 V -> A (in Ref. 3; BAC21666).
{ECO:0000305}.
CONFLICT 616 617 RT -> WS (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 652 652 I -> T (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 699 699 Q -> H (in Ref. 3; BAC21666).
{ECO:0000305}.
CONFLICT 703 703 F -> L (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 739 739 A -> T (in Ref. 3; BAC21665/BAC21666).
{ECO:0000305}.
CONFLICT 754 756 ALP -> LL (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 921 921 A -> T (in Ref. 3; BAC21666).
{ECO:0000305}.
CONFLICT 932 932 S -> N (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 1008 1008 D -> N (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 1078 1078 D -> A (in Ref. 3; BAC21666).
{ECO:0000305}.
CONFLICT 1094 1094 N -> T (in Ref. 3; BAC21666).
{ECO:0000305}.
CONFLICT 1159 1159 C -> R (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 1247 1247 E -> K (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 1256 1256 N -> D (in Ref. 3; BAC21665).
{ECO:0000305}.
CONFLICT 1258 1258 S -> F (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 1280 1283 APLY -> GPPS (in Ref. 2; AAD25540).
{ECO:0000305}.
CONFLICT 1433 1433 A -> V (in Ref. 2; AAD25540).
{ECO:0000305}.
SEQUENCE 1531 AA; 167499 MW; DFC4B60CCBC5529A CRC64;
MALTPQRGSS SGLSRPELWL LLWAAAWRLG ATACPALCTC TGTTVDCHGT GLQAIPKNIP
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ
LQVLPELLFQ NNQALSRLDL SENSLQAVPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT
QCSGPASLRG LNVAEVQKSE FSCSGQGEAA QVPACTLSSG SCPAMCSCSN GIVDCRGKGL
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TTGARCASPR RLANKRIGQI
KSKKFRCSAK EQYFIPGTED YHLNSECTSD VACPHKCRCE ASVVECSGLK LSKIPERIPQ
STTELRLNNN EISILEATGL FKKLSHLKKI NLSNNKVSEI EDGTFEGATS VSELHLTANQ
LESVRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNHIT TISPGAFDTL
QALSTLNLLA NPFNCNCQLA WLGDWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE
EGQEEVGCLP RPQCPQECAC LDTVVRCSNK HLQALPKGIP KNVTELYLDG NQFTLVPGQL
STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH
GNDVSTLQEG IFADVTSLSH LAIGANPLYC DCHLRWLSSW VKTGYKEPGI ARCAGPPEME
GKLLLTTPAK KFECQGPPSL AVQAKCDPCL SSPCQNQGTC HNDPLEVYRC TCPSGYKGRN
CEVSLDSCSS NPCGNGGTCH AQEGEDAGFT CSCPSGFEGL TCGMNTDDCV KHDCVNGGVC
VDGIGNYTCQ CPLQYTGRAC EQLVDFCSPD LNPCQHEAQC VGTPEGPRCE CVPGYTGDNC
SKNQDDCKDH QCQNGAQCVD EINSYACLCA EGYSGQLCEI PPAPRNSCEG TECQNGANCV
DQGSRPVCQC LPGFGGPECE KLLSVNFVDR DTYLQFTDLQ NWPRANITLQ VSTAEDNGIL
LYNGDNDHIA VELYQGHVRV SYDPGSYPSS AIYSAETIND GQFHTVELVT FDQMVNLSID
GGSPMTMDNF GKHYTLNSEA PLYVGGMPVD VNSAAFRLWQ ILNGTSFHGC IRNLYINNEL
QDFTKTQMKP GVVPGCEPCR KLYCLHGICQ PNATPGPVCH CEAGWGGLHC DQPVDGPCHG
HKCVHGKCVP LDALAYSCQC QDGYSGALCN QVGAVAEPCG GLQCLHGHCQ ASATRGAHCV
CSPGFSGELC EQESECRGDP VRDFHRVQRG YAICQTTRPL SWVECRGACP GQGCCQGLRL
KRRKLTFECS DGTSFAEEVE KPTKCGCAPC A


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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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