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Neural cell adhesion molecule 2 (N-CAM-2) (NCAM-2)

 NCAM2_HUMAN             Reviewed;         837 AA.
O15394; A8MQ06; B7Z841; Q7Z7F2;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
10-OCT-2018, entry version 171.
RecName: Full=Neural cell adhesion molecule 2;
Short=N-CAM-2;
Short=NCAM-2;
Flags: Precursor;
Name=NCAM2; Synonyms=NCAM21;
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 VARIANT PRO-350.
TISSUE=Brain;
PubMed=9226371; DOI=10.1006/geno.1997.4782;
Paoloni-Giacobino A., Chen H., Antonarakis S.E.;
"Cloning of a novel human neural cell adhesion molecule gene (NCAM2)
that maps to chromosome region 21q21 and is potentially involved in
Down syndrome.";
Genomics 43:43-51(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
GLYCOSYLATION AT ASN-445 AND ASN-562.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[6]
STRUCTURE BY NMR OF 486-591.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the fibronectin type-III domain of human neural
cell adhesion molecule 2.";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: May play important roles in selective fasciculation and
zone-to-zone projection of the primary olfactory axons.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-2679983, EBI-2679983;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15394-1; Sequence=Displayed;
Name=2;
IsoId=O15394-2; Sequence=VSP_056637, VSP_056638, VSP_056639;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed most strongly in adult and fetal
brain.
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EMBL; U75330; AAB80803.1; -; mRNA.
EMBL; AK302870; BAH13827.1; -; mRNA.
EMBL; AP001114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052946; AAH52946.1; -; mRNA.
CCDS; CCDS42910.1; -. [O15394-1]
RefSeq; NP_004531.2; NM_004540.3. [O15394-1]
RefSeq; XP_016883847.1; XM_017028358.1.
UniGene; Hs.473450; -.
PDB; 2DOC; NMR; -; A=486-591.
PDB; 2JLL; X-ray; 2.30 A; A=301-689.
PDB; 2KBG; NMR; -; A=592-693.
PDB; 2V5T; X-ray; 2.00 A; A=115-301.
PDB; 2VAJ; X-ray; 2.70 A; A=21-113.
PDB; 2WIM; X-ray; 3.00 A; A/B=19-301.
PDB; 2XY1; X-ray; 1.90 A; A=209-398.
PDB; 2XY2; X-ray; 1.77 A; A=19-207.
PDB; 2XYC; X-ray; 2.65 A; A=301-591.
PDBsum; 2DOC; -.
PDBsum; 2JLL; -.
PDBsum; 2KBG; -.
PDBsum; 2V5T; -.
PDBsum; 2VAJ; -.
PDBsum; 2WIM; -.
PDBsum; 2XY1; -.
PDBsum; 2XY2; -.
PDBsum; 2XYC; -.
ProteinModelPortal; O15394; -.
SMR; O15394; -.
BioGrid; 110765; 2.
DIP; DIP-56211N; -.
IntAct; O15394; 2.
STRING; 9606.ENSP00000383392; -.
GlyConnect; 1546; -.
iPTMnet; O15394; -.
PhosphoSitePlus; O15394; -.
SwissPalm; O15394; -.
BioMuta; NCAM2; -.
MaxQB; O15394; -.
PaxDb; O15394; -.
PeptideAtlas; O15394; -.
PRIDE; O15394; -.
ProteomicsDB; 48635; -.
Ensembl; ENST00000400546; ENSP00000383392; ENSG00000154654. [O15394-1]
GeneID; 4685; -.
KEGG; hsa:4685; -.
UCSC; uc002yld.3; human. [O15394-1]
CTD; 4685; -.
DisGeNET; 4685; -.
EuPathDB; HostDB:ENSG00000154654.14; -.
GeneCards; NCAM2; -.
H-InvDB; HIX0027799; -.
HGNC; HGNC:7657; NCAM2.
HPA; HPA030900; -.
HPA; HPA030901; -.
MIM; 602040; gene.
neXtProt; NX_O15394; -.
OpenTargets; ENSG00000154654; -.
PharmGKB; PA31460; -.
eggNOG; ENOG410IQJD; Eukaryota.
eggNOG; ENOG41118FG; LUCA.
GeneTree; ENSGT00910000144011; -.
HOGENOM; HOG000074124; -.
HOVERGEN; HBG052579; -.
InParanoid; O15394; -.
KO; K06491; -.
OMA; RITNHED; -.
OrthoDB; EOG091G00V0; -.
PhylomeDB; O15394; -.
TreeFam; TF326195; -.
ChiTaRS; NCAM2; human.
EvolutionaryTrace; O15394; -.
GenomeRNAi; 4685; -.
PRO; PR:O15394; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000154654; Expressed in 101 organ(s), highest expression level in corpus callosum.
CleanEx; HS_NCAM2; -.
ExpressionAtlas; O15394; baseline and differential.
Genevisible; O15394; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
GO; GO:0007158; P:neuron cell-cell adhesion; TAS:ProtInc.
GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR009138; Neural_cell_adh.
Pfam; PF00041; fn3; 2.
Pfam; PF07679; I-set; 4.
PRINTS; PR01838; NCAMFAMILY.
SMART; SM00060; FN3; 2.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 5.
SMART; SM00406; IGv; 3.
SUPFAM; SSF48726; SSF48726; 5.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS50835; IG_LIKE; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 837 Neural cell adhesion molecule 2.
/FTId=PRO_0000015018.
TOPO_DOM 20 697 Extracellular. {ECO:0000255}.
TRANSMEM 698 718 Helical. {ECO:0000255}.
TOPO_DOM 719 837 Cytoplasmic. {ECO:0000255}.
DOMAIN 21 108 Ig-like C2-type 1.
DOMAIN 113 202 Ig-like C2-type 2.
DOMAIN 208 297 Ig-like C2-type 3.
DOMAIN 302 396 Ig-like C2-type 4.
DOMAIN 401 491 Ig-like C2-type 5.
DOMAIN 498 591 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 593 688 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOD_RES 765 765 Phosphoserine.
{ECO:0000250|UniProtKB:O35136}.
MOD_RES 780 780 Phosphothreonine.
{ECO:0000250|UniProtKB:O35136}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000250|UniProtKB:O35136}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 419 419 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519}.
CARBOHYD 474 474 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 562 562 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519}.
DISULFID 42 93 {ECO:0000305}.
DISULFID 136 186 {ECO:0000305}.
DISULFID 232 281 {ECO:0000305}.
DISULFID 322 380 {ECO:0000305}.
DISULFID 422 475 {ECO:0000305}.
VAR_SEQ 1 18 MSLLLSFYLLGLLVSSGQ -> MVRSDSGGQVYLDYHNRQG
LFVDWKYNEALYLEEGQPETYYRT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056637.
VAR_SEQ 399 399 Y -> S (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056638.
VAR_SEQ 400 837 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056639.
VARIANT 347 347 D -> N (in dbSNP:rs35654962).
/FTId=VAR_047897.
VARIANT 350 350 L -> P (in dbSNP:rs232518).
{ECO:0000269|PubMed:9226371}.
/FTId=VAR_047898.
CONFLICT 49 49 E -> R (in Ref. 1; AAB80803).
{ECO:0000305}.
CONFLICT 72 72 E -> G (in Ref. 1; AAB80803).
{ECO:0000305}.
CONFLICT 163 163 F -> L (in Ref. 1; AAB80803).
{ECO:0000305}.
CONFLICT 374 374 D -> G (in Ref. 1; AAB80803).
{ECO:0000305}.
CONFLICT 662 667 YEVQIT -> MKFRLP (in Ref. 1; AAB80803).
{ECO:0000305}.
STRAND 20 26 {ECO:0000244|PDB:2XY2}.
STRAND 28 33 {ECO:0000244|PDB:2XY2}.
STRAND 38 46 {ECO:0000244|PDB:2XY2}.
STRAND 49 54 {ECO:0000244|PDB:2XY2}.
STRAND 65 72 {ECO:0000244|PDB:2XY2}.
STRAND 75 80 {ECO:0000244|PDB:2XY2}.
HELIX 85 87 {ECO:0000244|PDB:2XY2}.
STRAND 89 96 {ECO:0000244|PDB:2XY2}.
STRAND 98 100 {ECO:0000244|PDB:2WIM}.
STRAND 102 112 {ECO:0000244|PDB:2XY2}.
STRAND 116 119 {ECO:0000244|PDB:2V5T}.
STRAND 123 127 {ECO:0000244|PDB:2XY2}.
STRAND 132 134 {ECO:0000244|PDB:2XY2}.
STRAND 137 139 {ECO:0000244|PDB:2V5T}.
STRAND 145 150 {ECO:0000244|PDB:2XY2}.
STRAND 152 154 {ECO:0000244|PDB:2XY2}.
STRAND 163 165 {ECO:0000244|PDB:2XY2}.
STRAND 171 173 {ECO:0000244|PDB:2XY2}.
HELIX 178 180 {ECO:0000244|PDB:2XY2}.
STRAND 182 190 {ECO:0000244|PDB:2XY2}.
TURN 191 194 {ECO:0000244|PDB:2XY2}.
STRAND 195 206 {ECO:0000244|PDB:2XY2}.
STRAND 210 212 {ECO:0000244|PDB:2XY1}.
STRAND 217 221 {ECO:0000244|PDB:2XY1}.
STRAND 222 224 {ECO:0000244|PDB:2WIM}.
STRAND 228 231 {ECO:0000244|PDB:2XY1}.
STRAND 233 235 {ECO:0000244|PDB:2XY1}.
STRAND 241 246 {ECO:0000244|PDB:2XY1}.
STRAND 254 260 {ECO:0000244|PDB:2XY1}.
TURN 261 264 {ECO:0000244|PDB:2XY1}.
STRAND 265 268 {ECO:0000244|PDB:2XY1}.
HELIX 273 275 {ECO:0000244|PDB:2XY1}.
STRAND 277 285 {ECO:0000244|PDB:2XY1}.
STRAND 288 307 {ECO:0000244|PDB:2XY1}.
STRAND 310 312 {ECO:0000244|PDB:2XY1}.
STRAND 317 328 {ECO:0000244|PDB:2XY1}.
STRAND 331 336 {ECO:0000244|PDB:2XY1}.
TURN 337 340 {ECO:0000244|PDB:2XY1}.
STRAND 341 343 {ECO:0000244|PDB:2XY1}.
STRAND 350 352 {ECO:0000244|PDB:2XYC}.
STRAND 354 359 {ECO:0000244|PDB:2XY1}.
STRAND 362 369 {ECO:0000244|PDB:2XY1}.
HELIX 372 374 {ECO:0000244|PDB:2XY1}.
STRAND 376 384 {ECO:0000244|PDB:2XY1}.
STRAND 387 397 {ECO:0000244|PDB:2XY1}.
STRAND 409 412 {ECO:0000244|PDB:2JLL}.
STRAND 418 422 {ECO:0000244|PDB:2JLL}.
STRAND 424 428 {ECO:0000244|PDB:2JLL}.
STRAND 431 436 {ECO:0000244|PDB:2JLL}.
STRAND 439 442 {ECO:0000244|PDB:2JLL}.
STRAND 449 453 {ECO:0000244|PDB:2JLL}.
STRAND 458 462 {ECO:0000244|PDB:2JLL}.
STRAND 469 479 {ECO:0000244|PDB:2JLL}.
STRAND 482 492 {ECO:0000244|PDB:2JLL}.
STRAND 500 507 {ECO:0000244|PDB:2JLL}.
STRAND 512 517 {ECO:0000244|PDB:2JLL}.
STRAND 527 536 {ECO:0000244|PDB:2JLL}.
STRAND 543 546 {ECO:0000244|PDB:2JLL}.
STRAND 548 550 {ECO:0000244|PDB:2DOC}.
STRAND 552 556 {ECO:0000244|PDB:2JLL}.
STRAND 564 575 {ECO:0000244|PDB:2JLL}.
STRAND 576 580 {ECO:0000244|PDB:2XYC}.
STRAND 584 587 {ECO:0000244|PDB:2JLL}.
STRAND 599 604 {ECO:0000244|PDB:2JLL}.
TURN 605 607 {ECO:0000244|PDB:2JLL}.
STRAND 608 613 {ECO:0000244|PDB:2JLL}.
STRAND 619 621 {ECO:0000244|PDB:2KBG}.
STRAND 625 631 {ECO:0000244|PDB:2JLL}.
STRAND 640 645 {ECO:0000244|PDB:2KBG}.
TURN 646 648 {ECO:0000244|PDB:2KBG}.
STRAND 650 653 {ECO:0000244|PDB:2JLL}.
STRAND 661 670 {ECO:0000244|PDB:2JLL}.
STRAND 678 683 {ECO:0000244|PDB:2JLL}.
SEQUENCE 837 AA; 93046 MW; 878EC1110562B3F3 CRC64;
MSLLLSFYLL GLLVSSGQAL LQVTISLSKV ELSVGESKFF TCTAIGEPES IDWYNPQGEK
IISTQRVVVQ KEGVRSRLTI YNANIEDAGI YRCQATDAKG QTQEATVVLE IYQKLTFREV
VSPQEFKQGE DAEVVCRVSS SPAPAVSWLY HNEEVTTISD NRFAMLANNN LQILNINKSD
EGIYRCEGRV EARGEIDFRD IIVIVNVPPA ISMPQKSFNA TAERGEEMTF SCRASGSPEP
AISWFRNGKL IEENEKYILK GSNTELTVRN IINSDGGPYV CRATNKAGED EKQAFLQVFV
QPHIIQLKNE TTYENGQVTL VCDAEGEPIP EITWKRAVDG FTFTEGDKSL DGRIEVKGQH
GSSSLHIKDV KLSDSGRYDC EAASRIGGHQ KSMYLDIEYA PKFISNQTIY YSWEGNPINI
SCDVKSNPPA SIHWRRDKLV LPAKNTTNLK TYSTGRKMIL EIAPTSDNDF GRYNCTATNH
IGTRFQEYIL ALADVPSSPY GVKIIELSQT TAKVSFNKPD SHGGVPIHHY QVDVKEVASE
IWKIVRSHGV QTMVVLNNLE PNTTYEIRVA AVNGKGQGDY SKIEIFQTLP VREPSPPSIH
GQPSSGKSFK LSITKQDDGG APILEYIVKY RSKDKEDQWL EKKVQGNKDH IILEHLQWTM
GYEVQITAAN RLGYSEPTVY EFSMPPKPNI IKDTLFNGLG LGAVIGLGVA ALLLILVVTD
VSCFFIRQCG LLMCITRRMC GKKSGSSGKS KELEEGKAAY LKDGSKEPIV EMRTEDERVT
NHEDGSPVNE PNETTPLTEP EKLPLKEEDG KEALNPETIE IKVSNDIIQS KEDDSKA


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Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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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
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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
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


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81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

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GENTAUR Italy
SRL IVA IT03841300167
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Fax 02 36 00 65 94
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