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

Neural cell adhesion molecule L1-like protein (Close homolog of L1) [Cleaved into: Processed neural cell adhesion molecule L1-like protein]

 NCHL1_HUMAN             Reviewed;        1208 AA.
O00533; B7ZL03; Q2M3G2; Q59FY0;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
12-SEP-2018, entry version 150.
RecName: Full=Neural cell adhesion molecule L1-like protein;
AltName: Full=Close homolog of L1;
Contains:
RecName: Full=Processed neural cell adhesion molecule L1-like protein;
Flags: Precursor;
Name=CHL1; Synonyms=CALL;
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 SPECIFICITY, AND
VARIANTS ALA-287 AND VAL-1034.
PubMed=9799093; DOI=10.1007/s004390050829;
Wei M.-H., Karavanova I., Ivanov S.V., Popescu N.C., Keck C.L.,
Pack S., Eisen J.A., Lerman M.I.;
"In silico-initiated cloning and molecular characterization of a novel
human member of the L1 gene family of neural cell adhesion
molecules.";
Hum. Genet. 103:355-364(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-287 AND VAL-1034.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-287 AND VAL-1034.
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 [LARGE SCALE ANALYSIS] AT ASN-476; ASN-482; ASN-562;
ASN-767; ASN-822 AND ASN-1026.
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).
[6]
VARIANT [LARGE SCALE ANALYSIS] ILE-411.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Extracellular matrix and cell adhesion protein that
plays a role in nervous system development and in synaptic
plasticity. Both soluble and membranous forms promote neurite
outgrowth of cerebellar and hippocampal neurons and suppress
neuronal cell death. Plays a role in neuronal positioning of
pyramidal neurons and in regulation of both the number of
interneurons and the efficacy of GABAergic synapses. May play a
role in regulating cell migration in nerve regeneration and
cortical development. Potentiates integrin-dependent cell
migration towards extracellular matrix proteins. Recruits ANK3 to
the plasma membrane (By similarity). {ECO:0000250}.
-!- SUBUNIT: May interact with L1CAM. May interact with ITGB1/ITGA1
heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=Soluble forms produced
by cleavage/shedding also exist. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed neural cell adhesion molecule L1-
like protein: Secreted, extracellular space, extracellular matrix
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O00533-1; Sequence=Displayed;
Name=2;
IsoId=O00533-2; Sequence=VSP_020082;
Note=Contains a N-linked (GlcNAc...) asparagine at position 231.
{ECO:0000255};
-!- TISSUE SPECIFICITY: Expressed in the fetal and adult brain as well
as in Schwann cell culture. Also detected in adult peripheral
tissues. {ECO:0000269|PubMed:9799093}.
-!- DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment
region.
-!- DOMAIN: The DGEA motif seems to be a recognition site for
integrin.
-!- PTM: Cleavage by metalloprotease ADAM8 in the extracellular part
generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is
inhibited by metalloprotease inhibitors.
-!- PTM: N-glycosylated. Contains N-linked oligosaccharides with a
sulfated carbohydrate structure type HNK-1 (SO4-3-
GlcUABeta1,3GalBeta1,4GlcNAc) (By similarity). {ECO:0000250}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
L1/neurofascin/NgCAM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92566.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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; AF002246; AAB60937.1; -; mRNA.
EMBL; AB209329; BAD92566.1; ALT_INIT; mRNA.
EMBL; AC011609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC104918; AAI04919.1; -; mRNA.
EMBL; BC143496; AAI43497.1; -; mRNA.
CCDS; CCDS2556.1; -. [O00533-2]
CCDS; CCDS58812.1; -. [O00533-1]
RefSeq; NP_001240316.1; NM_001253387.1. [O00533-1]
RefSeq; NP_006605.2; NM_006614.3. [O00533-2]
RefSeq; XP_006713001.1; XM_006712938.1. [O00533-2]
RefSeq; XP_006713002.1; XM_006712939.3. [O00533-2]
RefSeq; XP_006713003.1; XM_006712940.3. [O00533-2]
RefSeq; XP_011531594.1; XM_011533292.1. [O00533-2]
RefSeq; XP_011531596.1; XM_011533294.1. [O00533-1]
RefSeq; XP_011531597.1; XM_011533295.1. [O00533-1]
RefSeq; XP_016861055.1; XM_017005566.1. [O00533-2]
RefSeq; XP_016861056.1; XM_017005567.1. [O00533-2]
RefSeq; XP_016861057.1; XM_017005568.1. [O00533-2]
RefSeq; XP_016861058.1; XM_017005569.1. [O00533-1]
RefSeq; XP_016861059.1; XM_017005570.1. [O00533-1]
RefSeq; XP_016861060.1; XM_017005571.1. [O00533-1]
UniGene; Hs.148909; -.
UniGene; Hs.731409; -.
ProteinModelPortal; O00533; -.
SMR; O00533; -.
BioGrid; 115975; 4.
IntAct; O00533; 2.
STRING; 9606.ENSP00000256509; -.
iPTMnet; O00533; -.
PhosphoSitePlus; O00533; -.
SwissPalm; O00533; -.
BioMuta; CHL1; -.
MaxQB; O00533; -.
PaxDb; O00533; -.
PeptideAtlas; O00533; -.
PRIDE; O00533; -.
ProteomicsDB; 47957; -.
ProteomicsDB; 47958; -. [O00533-2]
Ensembl; ENST00000256509; ENSP00000256509; ENSG00000134121. [O00533-2]
Ensembl; ENST00000397491; ENSP00000380628; ENSG00000134121. [O00533-1]
GeneID; 10752; -.
KEGG; hsa:10752; -.
UCSC; uc003bot.4; human. [O00533-1]
CTD; 10752; -.
DisGeNET; 10752; -.
EuPathDB; HostDB:ENSG00000134121.9; -.
GeneCards; CHL1; -.
H-InvDB; HIX0030810; -.
HGNC; HGNC:1939; CHL1.
HPA; CAB026120; -.
HPA; HPA003345; -.
MIM; 607416; gene.
neXtProt; NX_O00533; -.
OpenTargets; ENSG00000134121; -.
Orphanet; 1620; Distal monosomy 3p.
PharmGKB; PA26470; -.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00760000118840; -.
HOGENOM; HOG000231380; -.
HOVERGEN; HBG000144; -.
InParanoid; O00533; -.
KO; K06758; -.
OMA; YVRYQFR; -.
OrthoDB; EOG091G00LY; -.
PhylomeDB; O00533; -.
TreeFam; TF351098; -.
Reactome; R-HSA-447041; CHL1 interactions.
ChiTaRS; CHL1; human.
GeneWiki; CHL1; -.
GenomeRNAi; 10752; -.
PRO; PR:O00533; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000134121; Expressed in 204 organ(s), highest expression level in neocortex.
CleanEx; HS_CHL1; -.
ExpressionAtlas; O00533; baseline and differential.
Genevisible; O00533; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0050890; P:cognition; IEA:Ensembl.
GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 10.
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; IPR013151; Immunoglobulin.
InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
Pfam; PF13882; Bravo_FIGEY; 1.
Pfam; PF00041; fn3; 4.
Pfam; PF07679; I-set; 1.
Pfam; PF00047; ig; 1.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 6.
SMART; SM00408; IGc2; 5.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
Extracellular matrix; Glycoprotein; Immunoglobulin domain; Membrane;
Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1208 Neural cell adhesion molecule L1-like
protein.
/FTId=PRO_0000247896.
CHAIN 25 ? Processed neural cell adhesion molecule
L1-like protein. {ECO:0000255}.
/FTId=PRO_0000314777.
TOPO_DOM 25 1082 Extracellular. {ECO:0000255}.
TRANSMEM 1083 1103 Helical. {ECO:0000255}.
TOPO_DOM 1104 1208 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 124 Ig-like C2-type 1.
DOMAIN 128 223 Ig-like C2-type 2.
DOMAIN 235 328 Ig-like C2-type 3.
DOMAIN 331 417 Ig-like C2-type 4.
DOMAIN 423 510 Ig-like C2-type 5.
DOMAIN 515 607 Ig-like C2-type 6.
DOMAIN 614 709 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 714 807 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 809 914 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 918 1015 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 555 558 DGEA.
MOTIF 1181 1185 FIG[AQ]Y.
SITE 753 754 Cleavage; by ADAM8. {ECO:0000250}.
SITE 1039 1040 Cleavage; by ADAM8. {ECO:0000250}.
MOD_RES 1147 1147 Phosphoserine.
{ECO:0000250|UniProtKB:P70232}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000250|UniProtKB:P70232}.
MOD_RES 1180 1180 Phosphoserine.
{ECO:0000250|UniProtKB:P70232}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 562 562 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 767 767 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 822 822 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1026 1026 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 57 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 153 204 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 262 310 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 352 401 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 445 494 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 536 591 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 227 227 S -> LKHANDSSSSTEIGSKA (in isoform 2).
{ECO:0000303|PubMed:9799093}.
/FTId=VSP_020082.
VARIANT 17 17 L -> F (in dbSNP:rs2272522).
/FTId=VAR_027167.
VARIANT 287 287 T -> A (in dbSNP:rs13060847).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9799093,
ECO:0000269|Ref.2}.
/FTId=VAR_027168.
VARIANT 411 411 L -> I (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035505.
VARIANT 1034 1034 I -> V (in dbSNP:rs6442827).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9799093,
ECO:0000269|Ref.2}.
/FTId=VAR_027169.
SEQUENCE 1208 AA; 135071 MW; F706F87B60A1685D CRC64;
MEPLLLGRGL IVYLMFLLLK FSKAIEIPSS VQQVPTIIKQ SKVQVAFPFD EYFQIECEAK
GNPEPTFSWT KDGNPFYFTD HRIIPSNNSG TFRIPNEGHI SHFQGKYRCF ASNKLGIAMS
EEIEFIVPSV PKFPKEKIDP LEVEEGDPIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV
YMSQKGDLYF ANVEEKDSRN DYCCFAAFPR LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP
PTESGSESSI TILKGEILLL ECFAEGLPTP QVDWNKIGGD LPKGRETKEN YGKTLKIENV
SYQDKGNYRC TASNFLGTAT HDFHVIVEEP PRWTKKPQSA VYSTGSNGIL LCEAEGEPQP
TIKWRVNGSP VDNHPFAGDV VFPREISFTN LQPNHTAVYQ CEASNVHGTI LANANIDVVD
VRPLIQTKDG ENYATVVGYS AFLHCEFFAS PEAVVSWQKV EEVKPLEGRR YHIYENGTLQ
INRTTEEDAG SYSCWVENAI GKTAVTANLD IRNATKLRVS PKNPRIPKLH MLELHCESKC
DSHLKHSLKL SWSKDGEAFE INGTEDGRII IDGANLTISN VTLEDQGIYC CSAHTALDSA
ADITQVTVLD VPDPPENLHL SERQNRSVRL TWEAGADHNS NISEYIVEFE GNKEEPGRWE
ELTRVQGKKT TVILPLAPFV RYQFRVIAVN EVGRSQPSQP SDHHETPPAA PDRNPQNIRV
QASQPKEMII KWEPLKSMEQ NGPGLEYRVT WKPQGAPVEW EEETVTNHTL RVMTPAVYAP
YDVKVQAINQ LGSGPDPQSV TLYSGEDYPD TAPVIHGVDV INSTLVKVTW STVPKDRVHG
RLKGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDAFSEFHL TVLAYNSKGA
GPESEPYIFQ TPEGVPEQPT FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY
EIGELNDINI TTPSKPSWHL SNLNATTKYK FYLRACTSQG CGKPITEESS TLGEGSKGIG
KISGVNLTQK THPIEVFEPG AEHIVRLMTK NWGDNDSIFQ DVIETRGREY AGLYDDISTQ
GWFIGLMCAI ALLTLLLLTV CFVKRNRGGK YSVKEKEDLH PDPEIQSVKD ETFGEYSDSD
EKPLKGSLRS LNRDMQPTES ADSLVEYGEG DHGLFSEDGS FIGAYAGSKE KGSVESNGSS
TATFPLRA


Related products :

Catalog number Product name Quantity
EIAAB07193 Call,Cell adhesion molecule with homology to L1CAM,Chl1,Chl1-like protein,Close homolog of L1,Mouse,Mus musculus,Neural cell adhesion molecule L1-like protein
EIAAB07192 CALL,CHL1,Close homolog of L1,Homo sapiens,Human,Neural cell adhesion molecule L1-like protein
E1235m ELISA Mouse,Mus musculus,Ncam2,N-CAM-2,NCAM-2,Neural cell adhesion molecule 2,Neural cell adhesion molecule RB-8,Ocam,R4B12,Rncam 96T
E1235m ELISA kit Mouse,Mus musculus,Ncam2,N-CAM-2,NCAM-2,Neural cell adhesion molecule 2,Neural cell adhesion molecule RB-8,Ocam,R4B12,Rncam 96T
U1235m CLIA Mouse,Mus musculus,Ncam2,N-CAM-2,NCAM-2,Neural cell adhesion molecule 2,Neural cell adhesion molecule RB-8,Ocam,R4B12,Rncam 96T
PE094344h Recombinant human Neural cell adhesion molecule 1 protein 50ug
PE094344h Recombinant human Neural cell adhesion molecule 1 protein 1mg
PE094344h Recombinant human Neural cell adhesion molecule 1 protein 5mg
PE094344h Recombinant human Neural cell adhesion molecule 1 protein 200ug
CSB-RP074394h(C) Recombinant human Neural cell adhesion molecule L1 protein 500ug
CSB-EL005355HU Human Neural cell adhesion molecule L1-like protein(CHL1) ELISA kit 96T
CSB-EL005355MO Mouse Neural cell adhesion molecule L1-like protein(CHL1) ELISA kit 96T
CSB-EL005355MO Mouse Neural cell adhesion molecule L1-like protein(CHL1) ELISA kit SpeciesMouse 96T
CSB-RP074394h(C) Recombinant human Neural cell adhesion molecule L1 protein Source: E.coli 1mg
CSB-EL005355HU Human Neural cell adhesion molecule L1-like protein(CHL1) ELISA kit SpeciesHuman 96T
CHL1_MOUSE ELISA Kit FOR Neural cell adhesion molecule L1-like protein; organism: Mouse; gene name: Chl1 96T
bs-0736P Peptides: CD56_NCAM1 (Neural Cell Adhesion Molecule 1) Protein Length:12-25 amino acids. 200ug lyophilized
bs-0805P Peptides: CD56_NCAM1(Neural Cell Adhesion Molecule 1) Protein Length:12-25 amino acids. 200ug lyophilized
EIAAB27851 Ankyrin-binding cell adhesion molecule NrCAM,Neuronal cell adhesion molecule,Neuronal surface protein Bravo,Ng-CAM-related,NgCAM-related cell adhesion molecule,Nrcam,Nr-CAM,Rat,Rattus norvegicus,rBrav
MC-740 Neural Cell Adhesion Molecule mAb 1 mL
MC-740 Neural Cell Adhesion Molecule mAb 1 mL
MC-740 Neural Cell Adhesion Molecule mAb 123C3 1 mL
EH666 Neural cell adhesion molecule 1 Elisa Kit 96T
EH1411 Neural cell adhesion molecule 2 Elisa Kit 96T
Y100059 NCAM_2 (Neural Cell Adhesion Molecule 2) 100ug


 

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