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

CD9 antigen (5H9 antigen) (Cell growth-inhibiting gene 2 protein) (Leukocyte antigen MIC3) (Motility-related protein) (MRP-1) (Tetraspanin-29) (Tspan-29) (p24) (CD antigen CD9)

 CD9_HUMAN               Reviewed;         228 AA.
P21926; D3DUQ9; Q5J7W6; Q96ES4;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
12-SEP-2018, entry version 187.
RecName: Full=CD9 antigen;
AltName: Full=5H9 antigen;
AltName: Full=Cell growth-inhibiting gene 2 protein;
AltName: Full=Leukocyte antigen MIC3;
AltName: Full=Motility-related protein;
Short=MRP-1;
AltName: Full=Tetraspanin-29;
Short=Tspan-29;
AltName: Full=p24;
AltName: CD_antigen=CD9;
Name=CD9; Synonyms=MIC3, TSPAN29; ORFNames=GIG2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-5.
PubMed=1840589;
Boucheix C., Benoit P., Frachet P., Billard M., Worthington R.E.,
Gagnon J., Uzan G.;
"Molecular cloning of the CD9 antigen. A new family of cell surface
proteins.";
J. Biol. Chem. 266:117-122(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2037603;
Lanza F., Wolf D., Fox C.F., Kieffer N., Seyer J.M., Fried V.A.,
Coughlin S.R., Phillips D.R., Jennings L.K.;
"cDNA cloning and expression of platelet p24/CD9. Evidence for a new
family of multiple membrane-spanning proteins.";
J. Biol. Chem. 266:10638-10645(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1720807; DOI=10.1084/jem.174.6.1347;
Miyake M., Koyama M., Seno M., Ikeyama S.;
"Identification of the motility-related protein (MRP-1), recognized by
monoclonal antibody M31-15, which inhibits cell motility.";
J. Exp. Med. 174:1347-1354(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=8486348; DOI=10.1006/geno.1993.1150;
Rubinstein E., Benoit P., Billard M., Plaisance S., Prenant M.,
Uzan G., Boucheix C.;
"Organization of the human CD9 gene.";
Genomics 16:132-138(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15196249; DOI=10.1111/j.1365-2249.2004.02494.x;
Kobayashi H., Hosono O., Iwata S., Kawasaki H., Kuwana M., Tanaka H.,
Dang N.H., Morimoto C.;
"The tetraspanin CD9 is preferentially expressed on the human
CD4(+)CD45RA+ naive T cell population and is involved in T cell
activation.";
Clin. Exp. Immunol. 137:101-108(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human growth inhibition gene 2 (GIG2).";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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).
[10]
PROTEIN SEQUENCE OF 2-21.
TISSUE=Platelet;
PubMed=2358073; DOI=10.1016/0014-5793(90)80265-K;
Higashihara M., Takahata K., Yatomi Y., Nakahara K., Kurokawa K.;
"Purification and partial characterization of CD9 antigen of human
platelets.";
FEBS Lett. 264:270-274(1990).
[11]
ROLE IN CELL MOTILITY AND METASTASIS.
PubMed=8478605; DOI=10.1084/jem.177.5.1231;
Ikeyama S., Koyama M., Yamaoko M., Sasada R., Miyake M.;
"Suppression of cell motility and metastasis by transfection with
human motility-related protein (MRP-1/CD9) DNA.";
J. Exp. Med. 177:1231-1237(1993).
[12]
ROLE IN CELL ADHESION.
PubMed=7511626;
Masellis-Smith A., Shaw A.R.;
"CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B
cell adhesion to bone marrow fibroblasts through de novo recognition
of fibronectin.";
J. Immunol. 152:2768-2777(1994).
[13]
ROLE IN SPERM-EGG FUSION.
PubMed=14575715; DOI=10.1016/j.bbrc.2003.09.196;
Higginbottom A., Takahashi Y., Bolling L., Coonrod S.A., White J.M.,
Partridge L.J., Monk P.N.;
"Structural requirements for the inhibitory action of the CD9 large
extracellular domain in sperm/oocyte binding and fusion.";
Biochem. Biophys. Res. Commun. 311:208-214(2003).
[14]
SUBUNIT.
PubMed=14556650; DOI=10.1042/BJ20031037;
Kovalenko O.V., Yang X., Kolesnikova T.V., Hemler M.E.;
"Evidence for specific tetraspanin homodimers: inhibition of
palmitoylation makes cysteine residues available for cross-linking.";
Biochem. J. 377:407-417(2004).
[15]
PALMITOYLATION AT CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219,
AND MUTAGENESIS OF CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219.
PubMed=11959120; DOI=10.1016/S0014-5793(02)02522-X;
Charrin S., Manie S., Oualid M., Billard M., Boucheix C.,
Rubinstein E.;
"Differential stability of tetraspanin/tetraspanin interactions: role
of palmitoylation.";
FEBS Lett. 516:139-144(2002).
[16]
INTERACTION WITH PTGFRN.
PubMed=11278880; DOI=10.1074/jbc.M011297200;
Charrin S., Le Naour F., Oualid M., Billard M., Faure G., Hanash S.M.,
Boucheix C., Rubinstein E.;
"The major CD9 and CD81 molecular partner. Identification and
characterization of the complexes.";
J. Biol. Chem. 276:14329-14337(2001).
[17]
INTERACTION WITH IGSF8.
PubMed=11504738; DOI=10.1074/jbc.M107338200;
Stipp C.S., Kolesnikova T.V., Hemler M.E.;
"EWI-2 is a major CD9 and CD81 partner and member of a novel Ig
protein subfamily.";
J. Biol. Chem. 276:40545-40554(2001).
[18]
INTERACTION WITH PDPN.
PubMed=18541721; DOI=10.1182/blood-2007-11-124693;
Nakazawa Y., Sato S., Naito M., Kato Y., Mishima K., Arai H.,
Tsuruo T., Fujita N.;
"Tetraspanin family member CD9 inhibits Aggrus/podoplanin-induced
platelet aggregation and suppresses pulmonary metastasis.";
Blood 112:1730-1739(2008).
[19]
PALMITOYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION
WITH CD63, AND IDENTIFICATION IN A COMPLEX WITH ITGB3 AND CD63.
PubMed=19640571; DOI=10.1016/j.thromres.2009.07.005;
Israels S.J., McMillan-Ward E.M.;
"Palmitoylation supports the association of tetraspanin CD63 with CD9
and integrin alphaIIbbeta3 in activated platelets.";
Thromb. Res. 125:152-158(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
DISULFIDE BONDS.
PubMed=25551757; DOI=10.1371/journal.pone.0116289;
Hulme R.S., Higginbottom A., Palmer J., Partridge L.J., Monk P.N.;
"Distinct regions of the large extracellular domain of tetraspanin CD9
are involved in the control of human multinucleated giant cell
formation.";
PLoS ONE 9:E116289-E116289(2014).
[22]
INTERACTION WITH INTEGRIN ITGAV:ITGB3.
PubMed=27993971; DOI=10.1042/BCJ20160998;
Yu J., Lee C.Y., Changou C.A., Cedano-Prieto D.M., Takada Y.K.,
Takada Y.;
"The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-
binding site of integrin alphavbeta3.";
Biochem. J. 474:589-596(2017).
-!- FUNCTION: Involved in platelet activation and aggregation.
Regulates paranodal junction formation. Involved in cell adhesion,
cell motility and tumor metastasis. Required for sperm-egg fusion.
{ECO:0000269|PubMed:14575715, ECO:0000269|PubMed:7511626,
ECO:0000269|PubMed:8478605}.
-!- SUBUNIT: Forms both disulfide-linked homodimers and higher
homooligomers as well as heterooligomers with other members of the
tetraspanin family. Interacts with CD63. Identified in a complex
with CD63 and ITGB3. Associates with CR2/CD21 and with
PTGFRN/CD9P1. Interacts directly with IGSF8. Interacts with PDPN;
this interaction is homophilic and attenuates platelet aggregation
and pulmonary metastasis induced by PDPN (PubMed:18541721).
Interacts (via the second extracellular domain) with integrin
ITGAV:ITGB3 (PubMed:27993971). {ECO:0000269|PubMed:11278880,
ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:14556650,
ECO:0000269|PubMed:18541721, ECO:0000269|PubMed:19640571,
ECO:0000269|PubMed:27993971}.
-!- INTERACTION:
P08473:MME; NbExp=6; IntAct=EBI-4280101, EBI-353759;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19640571};
Multi-pass membrane protein {ECO:0000269|PubMed:19640571}. Cell
membrane {ECO:0000269|PubMed:19640571}; Multi-pass membrane
protein {ECO:0000269|PubMed:19640571}.
-!- TISSUE SPECIFICITY: Detected in platelets (at protein level).
Expressed by a variety of hematopoietic and epithelial cells.
{ECO:0000269|PubMed:19640571}.
-!- PTM: Palmitoylated at a low, basal level in unstimulated
platelets. The level of palmitoylation increases when platelets
are activated by thrombin (in vitro). The protein exists in three
forms with molecular masses between 22 and 27 kDa, and is known to
carry covalently linked fatty acids.
{ECO:0000269|PubMed:11959120}.
-!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cd9/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CD9ID995ch12p13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M38690; AAA80320.1; -; mRNA.
EMBL; L34068; AAA59982.1; -; mRNA.
EMBL; X60111; CAA42708.1; -; mRNA.
EMBL; S60489; AAC60586.1; -; Genomic_DNA.
EMBL; S60462; AAC60586.1; JOINED; Genomic_DNA.
EMBL; S60463; AAC60586.1; JOINED; Genomic_DNA.
EMBL; S60464; AAC60586.1; JOINED; Genomic_DNA.
EMBL; S60700; AAC60586.1; JOINED; Genomic_DNA.
EMBL; S60699; AAC60586.1; JOINED; Genomic_DNA.
EMBL; S60465; AAC60586.1; JOINED; Genomic_DNA.
EMBL; S60472; AAC60586.1; JOINED; Genomic_DNA.
EMBL; L08118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L08119; AAA51954.1; ALT_SEQ; Genomic_DNA.
EMBL; L08120; AAA51955.1; ALT_SEQ; Genomic_DNA.
EMBL; L08121; AAA51956.1; -; Genomic_DNA.
EMBL; L08122; AAA51957.1; -; Genomic_DNA.
EMBL; L08123; AAA51958.1; -; Genomic_DNA.
EMBL; L08124; AAA51959.1; -; Genomic_DNA.
EMBL; L08125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB079244; BAE71132.1; -; mRNA.
EMBL; AY423720; AAS00483.1; -; mRNA.
EMBL; AY422198; AAQ87878.1; -; Genomic_DNA.
EMBL; CH471116; EAW88812.1; -; Genomic_DNA.
EMBL; CH471116; EAW88813.1; -; Genomic_DNA.
EMBL; BC011988; AAH11988.1; -; mRNA.
CCDS; CCDS8540.1; -.
PIR; A46123; A40402.
RefSeq; NP_001317241.1; NM_001330312.1.
RefSeq; NP_001760.1; NM_001769.3.
UniGene; Hs.114286; -.
UniGene; Hs.712104; -.
ProteinModelPortal; P21926; -.
BioGrid; 107366; 23.
CORUM; P21926; -.
DIP; DIP-1122N; -.
IntAct; P21926; 25.
MINT; P21926; -.
STRING; 9606.ENSP00000009180; -.
DrugBank; DB05398; C31G.
TCDB; 8.A.40.1.9; the tetraspanin (tetraspanin) family.
iPTMnet; P21926; -.
PhosphoSitePlus; P21926; -.
SwissPalm; P21926; -.
BioMuta; CD9; -.
DMDM; 231724; -.
EPD; P21926; -.
MaxQB; P21926; -.
PaxDb; P21926; -.
PeptideAtlas; P21926; -.
PRIDE; P21926; -.
ProteomicsDB; 53942; -.
DNASU; 928; -.
Ensembl; ENST00000009180; ENSP00000009180; ENSG00000010278.
Ensembl; ENST00000382518; ENSP00000371958; ENSG00000010278.
Ensembl; ENST00000538834; ENSP00000496639; ENSG00000010278.
GeneID; 928; -.
KEGG; hsa:928; -.
UCSC; uc001qnq.3; human.
CTD; 928; -.
DisGeNET; 928; -.
EuPathDB; HostDB:ENSG00000010278.11; -.
GeneCards; CD9; -.
HGNC; HGNC:1709; CD9.
HPA; CAB002490; -.
MIM; 143030; gene.
neXtProt; NX_P21926; -.
OpenTargets; ENSG00000010278; -.
PharmGKB; PA26247; -.
eggNOG; KOG3882; Eukaryota.
eggNOG; ENOG4111IRY; LUCA.
GeneTree; ENSGT00880000137858; -.
HOGENOM; HOG000230651; -.
HOVERGEN; HBG002324; -.
InParanoid; P21926; -.
KO; K06460; -.
OMA; EVFHNKF; -.
OrthoDB; EOG091G0K9H; -.
PhylomeDB; P21926; -.
TreeFam; TF352895; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1300652; Sperm:Oocyte Membrane Binding.
Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
ChiTaRS; CD9; human.
GeneWiki; CD9; -.
GenomeRNAi; 928; -.
PRO; PR:P21926; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000010278; Expressed in 236 organ(s), highest expression level in trigeminal ganglion.
CleanEx; HS_CD9; -.
ExpressionAtlas; P21926; baseline and differential.
Genevisible; P21926; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0051271; P:negative regulation of cellular component movement; IDA:UniProtKB.
GO; GO:0090331; P:negative regulation of platelet aggregation; IDA:UniProtKB.
GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
GO; GO:0030913; P:paranodal junction assembly; ISS:UniProtKB.
GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEA:Ensembl.
Gene3D; 1.10.1450.10; -; 1.
InterPro; IPR000301; Tetraspanin.
InterPro; IPR018499; Tetraspanin/Peripherin.
InterPro; IPR018503; Tetraspanin_CS.
InterPro; IPR008952; Tetraspanin_EC2_sf.
Pfam; PF00335; Tetraspannin; 1.
PIRSF; PIRSF002419; Tetraspanin; 1.
PRINTS; PR00259; TMFOUR.
SUPFAM; SSF48652; SSF48652; 1.
PROSITE; PS00421; TM4_1; 1.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Fertilization;
Glycoprotein; Lipoprotein; Membrane; Palmitate; Reference proteome;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1840589,
ECO:0000269|PubMed:2358073}.
CHAIN 2 228 CD9 antigen.
/FTId=PRO_0000219205.
TOPO_DOM 2 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 33 Helical. {ECO:0000255}.
TOPO_DOM 34 55 Extracellular. {ECO:0000255}.
TRANSMEM 56 76 Helical. {ECO:0000255}.
TOPO_DOM 77 87 Cytoplasmic. {ECO:0000255}.
TRANSMEM 88 111 Helical. {ECO:0000255}.
TOPO_DOM 112 195 Extracellular. {ECO:0000255}.
TRANSMEM 196 221 Helical. {ECO:0000255}.
TOPO_DOM 222 228 Cytoplasmic. {ECO:0000255}.
LIPID 9 9 S-palmitoyl cysteine.
{ECO:0000305|PubMed:11959120}.
LIPID 78 78 S-palmitoyl cysteine.
{ECO:0000305|PubMed:11959120}.
LIPID 79 79 S-palmitoyl cysteine.
{ECO:0000305|PubMed:11959120}.
LIPID 87 87 S-palmitoyl cysteine.
{ECO:0000305|PubMed:11959120}.
LIPID 218 218 S-palmitoyl cysteine.
{ECO:0000305|PubMed:11959120}.
LIPID 219 219 S-palmitoyl cysteine.
{ECO:0000305|PubMed:11959120}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 152 181 {ECO:0000269|PubMed:25551757}.
DISULFID 153 167 {ECO:0000269|PubMed:25551757}.
MUTAGEN 9 9 C->A: Loss of palmitoylation; when
associated with A-78; A-79; A-87; A-218
and A-219. {ECO:0000269|PubMed:11959120}.
MUTAGEN 78 78 C->A: Loss of palmitoylation; when
associated with A-9; A-79; A-87; A-218
and A-219. {ECO:0000269|PubMed:11959120}.
MUTAGEN 79 79 C->A: Loss of palmitoylation; when
associated with A-9; A-78; A-87; A-218
and A-219. {ECO:0000269|PubMed:11959120}.
MUTAGEN 87 87 C->A: Loss of palmitoylation; when
associated with A-9; A-78; A-79; A-218
and A-219. {ECO:0000269|PubMed:11959120}.
MUTAGEN 218 218 C->A: Loss of palmitoylation; when
associated with A-9; A-78; A-79; A-87 and
A-219. {ECO:0000269|PubMed:11959120}.
MUTAGEN 219 219 C->A: Loss of palmitoylation; when
associated with A-9; A-78; A-79; A-87 and
A-218. {ECO:0000269|PubMed:11959120}.
CONFLICT 215 215 M -> T (in Ref. 9; AAH11988).
{ECO:0000305}.
SEQUENCE 228 AA; 25416 MW; F68333E0C20611D8 CRC64;
MPVKGGTKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQETN NNNSSFYTGV
YILIGAGALM MLVGFLGCCG AVQESQCMLG LFFGFLLVIF AIEIAAAIWG YSHKDEVIKE
VQEFYKDTYN KLKTKDEPQR ETLKAIHYAL NCCGLAGGVE QFISDICPKK DVLETFTVKS
CPDAIKEVFD NKFHIIGAVG IGIAVVMIFG MIFSMILCCA IRRNREMV


Related products :

Catalog number Product name Quantity
EIAAB06405 5H9 antigen,CD9,CD9 antigen,Cell growth-inhibiting gene 2 protein,GIG2,Homo sapiens,Human,Leukocyte antigen MIC3,MIC3,Motility-related protein,MRP-1,p24,Tetraspanin-29,TSPAN29,Tspan-29
20-272-192352 CD9 - Mouse monoclonal [MEM - 61] to CD9; p24; Leukocyte antigen MIC3; Motility-related protein; MRP-1; Tetraspanin-29; Tspan-29 Monoclonal 0.1 mg
20-272-191881 CD9 - Mouse monoclonal [ALB 6] to CD9; p24; Leukocyte antigen MIC3; Motility-related protein; MRP-1; Tetraspanin-29; Tspan-29 Monoclonal 0.1 mg
20-272-191898 CD9 - Mouse monoclonal [MM2_57] to CD9; p24; Leukocyte antigen MIC3; Motility-related protein; MRP-1; Tetraspanin-29; Tspan-29 Monoclonal 0.1 mg
20-272-191667 CD9 (FITC) - Mouse monoclonal [MEM-61] to CD9 (FITC); p24; Leukocyte antigen MIC3; Motility-related protein; MRP-1; Tetraspanin-29; Tspan-29 Monoclonal 100 TESTS
EIAAB06394 C33 antigen,CD82,CD82 antigen,Homo sapiens,Human,IA4,Inducible membrane protein R2,KAI1,Metastasis suppressor Kangai-1,SAR2,ST6,Suppressor of tumorigenicity 6 protein,Tetraspanin-27,TSPAN27,Tspan-27
18-003-43704 Carcinoembryonic antigen-related cell adhesion molecule 6 - Normal cross-reacting antigen; Non-specific crossreacting antigen; CD66c antigen Polyclonal 0.1 mg Protein A
U0002r CLIA Activated leukocyte cell adhesion molecule,Alcam,CD166 antigen,HB2,KG-CAM,Protein MEMD,Rat,Rattus norvegicus,SB-10 antigen 96T
E0002r ELISA Activated leukocyte cell adhesion molecule,Alcam,CD166 antigen,HB2,KG-CAM,Protein MEMD,Rat,Rattus norvegicus,SB-10 antigen 96T
E0002r ELISA kit Activated leukocyte cell adhesion molecule,Alcam,CD166 antigen,HB2,KG-CAM,Protein MEMD,Rat,Rattus norvegicus,SB-10 antigen 96T
EIAAB06271 CD151,CD151 antigen,GP27,Homo sapiens,Human,Membrane glycoprotein SFA-1,PETA-3,Platelet-endothelial tetraspan antigen 3,Tetraspanin-24,TSPAN24,Tspan-24
15-288-22478 Carcinoembryonic antigen-related cell adhesion molecule 5 - Carcinoembryonic antigen; CEA; Meconium antigen 100; CD66e antigen Polyclonal 0.1 mg
15-288-22478 Carcinoembryonic antigen-related cell adhesion molecule 5 - Carcinoembryonic antigen; CEA; Meconium antigen 100; CD66e antigen Polyclonal 0.05 mg
EIAAB45453 AIE75,Antigen NY-CO-38_NY-CO-37,Autoimmune enteropathy-related antigen AIE-75,Harmonin,Homo sapiens,Human,Protein PDZ-73,Renal carcinoma antigen NY-REN-3,USH1C,Usher syndrome type-1C protein
EIAAB06358 CD53,Cell surface glycoprotein CD53,Homo sapiens,Human,Leukocyte surface antigen CD53,MOX44,Tetraspanin-25,TSPAN25,Tspan-25
EIAAB06324 CD37,Homo sapiens,Human,Leukocyte antigen CD37,Tetraspanin-26,TSPAN26,Tspan-26
EIAAB06392 26 kDa cell surface protein TAPA-1,CD81,CD81 antigen,Homo sapiens,Human,TAPA1,Target of the antiproliferative antibody 1,Tetraspanin-28,TSPAN28,Tspan-28
EIAAB06697 Carcinoembryonic antigen CGM6,Carcinoembryonic antigen-related cell adhesion molecule 8,CD67 antigen,CEACAM8,CGM6,Homo sapiens,Human,Non-specific cross-reacting antigen NCA-95
EIAAB06695 Carcinoembryonic antigen-related cell adhesion molecule 6,CEACAM6,Homo sapiens,Human,NCA,Non-specific crossreacting antigen,Normal cross-reacting antigen
EIAAB06373 CD63,CD63 antigen,Granulophysin,Homo sapiens,Human,LAMP-3,Lysosomal-associated membrane protein 3,Melanoma-associated antigen ME491,MLA1,Ocular melanoma-associated antigen,OMA81H,Tetraspanin-30,TSPAN3
CEACAM8 CEACAM6 Gene carcinoembryonic antigen-related cell adhesion molecule 6 (non-specific cross reacting antigen)
20-783-71526 MOUSE ANTI HUMAN CD84 - Signaling lymphocytic activation molecule 5; Leukocyte differentiation antigen CD84; CD84 antigen; Cell surface antigen MAX.3; Hly9-beta Monoclonal 0.2 mg
20-783-71529 MOUSE ANTI HUMAN CD84 RPE - Signaling lymphocytic activation molecule 5; Leukocyte differentiation antigen CD84; CD84 antigen; Cell surface antigen MAX.3; Hly9-beta Monoclonal 100 TESTS
20-783-71528 MOUSE ANTI HUMAN CD84 FITC - Signaling lymphocytic activation molecule 5; Leukocyte differentiation antigen CD84; CD84 antigen; Cell surface antigen MAX.3; Hly9-beta Monoclonal 0.1 mg
20-783-71527 MOUSE ANTI HUMAN CD84 Biotin - Signaling lymphocytic activation molecule 5; Leukocyte differentiation antigen CD84; CD84 antigen; Cell surface antigen MAX.3; Hly9-beta Monoclonal 0.1 mg


 

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