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Cell adhesion molecule 3 (Brain immunoglobulin receptor) (Immunoglobulin superfamily member 4B) (IgSF4B) (Nectin-like protein 1) (NECL-1) (Synaptic cell adhesion molecule 3) (SynCAM3) (TSLC1-like protein 1) (TSLL1)

 CADM3_HUMAN             Reviewed;         398 AA.
Q8N126; Q8IZQ9; Q9NVJ5; Q9UJP1;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-MAY-2022, entry version 173.
RecName: Full=Cell adhesion molecule 3;
AltName: Full=Brain immunoglobulin receptor;
AltName: Full=Immunoglobulin superfamily member 4B;
Short=IgSF4B;
AltName: Full=Nectin-like protein 1;
Short=NECL-1;
AltName: Full=Synaptic cell adhesion molecule 3;
Short=SynCAM3;
AltName: Full=TSLC1-like protein 1;
Short=TSLL1;
Flags: Precursor;
Name=CADM3; Synonyms=IGSF4B, NECL1, SYNCAM3, TSLL1;
ORFNames=UNQ225/PRO258;
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), TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11536053; DOI=10.1038/sj.onc.1204696;
Fukuhara H., Kuramochi M., Nobukuni T., Fukami T., Saino M., Maruyama T.,
Nomura S., Sekiya T., Murakami Y.;
"Isolation of the TSLL1 and TSLL2 genes, members of the tumor suppressor
TSLC1 gene family encoding transmembrane proteins.";
Oncogene 20:5401-5407(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013;
Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B.,
Fan M., Peng X., Qiang B., Yuan J.;
"Nectin-like molecule 1 is a protein 4.1N associated protein and recruits
protein 4.1N from cytoplasm to the plasma membrane.";
Biochim. Biophys. Acta 1669:142-154(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Cunningham S.A., Tran T.M., Arrate M.P.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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], AND ALTERNATIVE SPLICING.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-280 (ISOFORM 3).
Keryanov S.A., Gardner K.L.;
"Alternatively splicing forms of the human nectin V gene.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified
cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-398.
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).
[9]
TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-290, AND LACK OF GLYCOSYLATION AT
ASN-25.
PubMed=18420026; DOI=10.1016/j.bbamem.2008.03.013;
Gao J., Chen T., Hu G., Gong Y., Qiang B., Yuan J., Peng X.;
"Nectin-like molecule 1 is a glycoprotein with a single N-glycosylation
site at N290KS which influences its adhesion activity.";
Biochim. Biophys. Acta 1778:1429-1435(2008).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-135, SUBUNIT, AND DISULFIDE
BOND.
PubMed=16467305; DOI=10.1074/jbc.m513459200;
Dong X., Xu F., Gong Y., Gao J., Lin P., Chen T., Peng Y., Qiang B.,
Yuan J., Peng X., Rao Z.;
"Crystal structure of the V domain of human Nectin-like molecule-
1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-
cell adhesion molecule.";
J. Biol. Chem. 281:10610-10617(2006).
-!- FUNCTION: Involved in the cell-cell adhesion. Has both calcium-
independent homophilic cell-cell adhesion activity and calcium-
independent heterophilic cell-cell adhesion activity with IGSF4,
NECTIN1 and NECTIN3. Interaction with EPB41L1 may regulate structure or
function of cell-cell junctions (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Can form trans-heterodimers with NECTIN3. Interacts
with EPB41L1, DLG3, PALS2 and CASK (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q8N126; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-18961338, EBI-2855401;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99N28};
Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99N28}.
Cell junction {ECO:0000250|UniProtKB:Q99N28}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N126-1; Sequence=Displayed;
Name=2;
IsoId=Q8N126-2; Sequence=VSP_017221;
Name=3;
IsoId=Q8N126-3; Sequence=VSP_022008;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed mainly in adult and fetal
brain. Isoform 2 is highly expressed in adult brain and weakly
expressed in placenta. In brain, Isoform 2 is highly expressed in
cerebellum. {ECO:0000269|PubMed:11536053, ECO:0000269|PubMed:15893517,
ECO:0000269|PubMed:18420026}.
-!- INDUCTION: Markedly in glioma cell lines and prostate cancer cell
lines. {ECO:0000269|PubMed:11536053}.
-!- DOMAIN: The cytoplasmic region mediates interaction with EPB41L1, DLG3,
PALS2 and CASK. {ECO:0000250}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AF363367; AAM60749.1; -; mRNA.
EMBL; AF062733; AAD17540.2; -; mRNA.
EMBL; AY046418; AAL02143.1; -; mRNA.
EMBL; AY358332; AAQ88698.1; -; mRNA.
EMBL; AL035403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF529206; AAN75603.1; -; mRNA.
EMBL; AK001560; BAA91756.1; ALT_INIT; mRNA.
CCDS; CCDS1182.1; -. [Q8N126-2]
CCDS; CCDS44251.1; -. [Q8N126-1]
RefSeq; NP_001120645.1; NM_001127173.2. [Q8N126-1]
RefSeq; NP_001333439.1; NM_001346510.1. [Q8N126-3]
RefSeq; NP_067012.1; NM_021189.4. [Q8N126-2]
PDB; 1Z9M; X-ray; 2.40 A; A/B=25-135.
PDBsum; 1Z9M; -.
AlphaFoldDB; Q8N126; -.
SMR; Q8N126; -.
BioGRID; 121793; 2.
IntAct; Q8N126; 1.
STRING; 9606.ENSP00000357106; -.
GlyGen; Q8N126; 2 sites, 1 O-linked glycan (1 site).
iPTMnet; Q8N126; -.
PhosphoSitePlus; Q8N126; -.
BioMuta; CADM3; -.
DMDM; 74759761; -.
EPD; Q8N126; -.
jPOST; Q8N126; -.
MassIVE; Q8N126; -.
MaxQB; Q8N126; -.
PeptideAtlas; Q8N126; -.
PRIDE; Q8N126; -.
ProteomicsDB; 71524; -. [Q8N126-1]
ProteomicsDB; 71525; -. [Q8N126-2]
ProteomicsDB; 71526; -. [Q8N126-3]
Antibodypedia; 669; 363 antibodies from 34 providers.
DNASU; 57863; -.
Ensembl; ENST00000368124.8; ENSP00000357106.4; ENSG00000162706.13. [Q8N126-2]
Ensembl; ENST00000368125.9; ENSP00000357107.4; ENSG00000162706.13.
GeneID; 57863; -.
KEGG; hsa:57863; -.
MANE-Select; ENST00000368125.9; ENSP00000357107.4; NM_001127173.3; NP_001120645.1.
UCSC; uc001ftk.3; human. [Q8N126-1]
CTD; 57863; -.
DisGeNET; 57863; -.
GeneCards; CADM3; -.
HGNC; HGNC:17601; CADM3.
HPA; ENSG00000162706; Tissue enhanced (brain, placenta).
MIM; 609743; gene.
neXtProt; NX_Q8N126; -.
OpenTargets; ENSG00000162706; -.
PharmGKB; PA162380906; -.
VEuPathDB; HostDB:ENSG00000162706; -.
eggNOG; ENOG502QWJ8; Eukaryota.
GeneTree; ENSGT00940000159779; -.
HOGENOM; CLU_047574_1_0_1; -.
InParanoid; Q8N126; -.
OMA; MTQERAL; -.
OrthoDB; 716894at2759; -.
PhylomeDB; Q8N126; -.
TreeFam; TF326804; -.
PathwayCommons; Q8N126; -.
Reactome; R-HSA-418990; Adherens junctions interactions.
Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
SignaLink; Q8N126; -.
BioGRID-ORCS; 57863; 9 hits in 1059 CRISPR screens.
ChiTaRS; CADM3; human.
EvolutionaryTrace; Q8N126; -.
GeneWiki; CADM3; -.
GenomeRNAi; 57863; -.
Pharos; Q8N126; Tbio.
PRO; PR:Q8N126; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; Q8N126; protein.
Bgee; ENSG00000162706; Expressed in cerebellar cortex and 196 other tissues.
ExpressionAtlas; Q8N126; baseline and differential.
Genevisible; Q8N126; HS.
GO; GO:0005911; C:cell-cell junction; ISS:HGNC-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:HGNC-UCL.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC-UCL.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR003585; Neurexin-like.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00294; 4.1m; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction;
Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1..24
/evidence="ECO:0000269|PubMed:15340161"
CHAIN 25..398
/note="Cell adhesion molecule 3"
/id="PRO_0000046067"
TOPO_DOM 25..330
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 331..351
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 352..398
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 25..126
/note="Ig-like V-type"
DOMAIN 130..228
/note="Ig-like C2-type 1"
DOMAIN 233..315
/note="Ig-like C2-type 2"
REGION 367..398
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
SITE 25
/note="Not glycosylated"
/evidence="ECO:0000269|PubMed:18420026"
MOD_RES 388
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q99N28"
CARBOHYD 290
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:18420026"
DISULFID 50..110
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:16467305"
DISULFID 152..209
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 254..299
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 29
/note="D -> DGYWQEQDLELGTLAPLDEAISSTVWSSPDMLASQ (in isoform
2)"
/evidence="ECO:0000303|PubMed:15893517"
/id="VSP_017221"
VAR_SEQ 185..231
/note="GKTFTVSSSVTFQVTREDDGASIVCSVNHESLKGADRSTSQRIEVLY -> D
(in isoform 3)"
/evidence="ECO:0000303|Ref.6"
/id="VSP_022008"
VARIANT 162
/note="R -> W (in dbSNP:rs3026987)"
/id="VAR_059383"
STRAND 38..41
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 46..51
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 60..63
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 69..72
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 83..88
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 90..97
/evidence="ECO:0007829|PDB:1Z9M"
HELIX 102..104
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 106..112
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 114..116
/evidence="ECO:0007829|PDB:1Z9M"
STRAND 118..127
/evidence="ECO:0007829|PDB:1Z9M"
SEQUENCE 398 AA; 43300 MW; 601B2FB5D512DB6C CRC64;
MGAPAASLLL LLLLFACCWA PGGANLSQDD SQPWTSDETV VAGGTVVLKC QVKDHEDSSL
QWSNPAQQTL YFGEKRALRD NRIQLVTSTP HELSISISNV ALADEGEYTC SIFTMPVRTA
KSLVTVLGIP QKPIITGYKS SLREKDTATL NCQSSGSKPA ARLTWRKGDQ ELHGEPTRIQ
EDPNGKTFTV SSSVTFQVTR EDDGASIVCS VNHESLKGAD RSTSQRIEVL YTPTAMIRPD
PPHPREGQKL LLHCEGRGNP VPQQYLWEKE GSVPPLKMTQ ESALIFPFLN KSDSGTYGCT
ATSNMGSYKA YYTLNVNDPS PVPSSSSTYH AIIGGIVAFI VFLLLIMLIF LGHYLIRHKG
TYLTHEAKGS DDAPDADTAI INAEGGQSGG DDKKEYFI


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25-998 IGSF11 functions as a cell adhesion molecule through homophilic interaction. IGSF11 stimulates cell growth.IGSF11 is an immunoglobulin (Ig) superfamily member that is preferentially expressed in brain 0.05 mg
32-131 CD31, also known as platelet endothelial cell adhesion molecule 1 (PECAM1), is a type I integral membrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors.It is co 0.1 mL
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
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
EIAAB11953 Down syndrome cell adhesion molecule 2,Down syndrome cell adhesion molecule-like protein 1,DSCAM2,DSCAML1,Homo sapiens,Human,KIAA1132
E0086r ELISA kit CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte 96T
U0086m CLIA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly22,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte 96T
U0086r CLIA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte antig 96T
U0086b CLIA Bos taurus,Bovine,CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,L-selectin,Lymph node homing receptor,SELL 96T
E0086m ELISA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly22,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte 96T
E0086b ELISA Bos taurus,Bovine,CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,L-selectin,Lymph node homing receptor,SELL 96T
E0086r ELISA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte anti 96T