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Sialoadhesin (Sheep erythrocyte receptor) (SER) (Sialic acid-binding Ig-like lectin 1) (Siglec-1) (CD antigen CD169)

 SN_MOUSE                Reviewed;        1695 AA.
Q62230; D3YVZ3; D3YVZ4; O55216; Q62228; Q62229;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 2.
30-AUG-2017, entry version 158.
RecName: Full=Sialoadhesin;
AltName: Full=Sheep erythrocyte receptor;
Short=SER;
AltName: Full=Sialic acid-binding Ig-like lectin 1;
Short=Siglec-1;
AltName: CD_antigen=CD169;
Flags: Precursor;
Name=Siglec1; Synonyms=Sa, Sn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND PARTIAL PROTEIN
SEQUENCE.
STRAIN=C57BL/6J; TISSUE=Macrophage;
PubMed=7925291;
Crocker P.R., Mucklow S., Boukson V., McWilliam A., Willis A.C.,
Gordon S., Milon G., Kelm S., Bradfield P.;
"Sialoadhesin, a macrophage sialic acid binding receptor for
haemopoietic cells with 17 immunoglobulin-like domains.";
EMBO J. 13:4490-4503(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9383289; DOI=10.1007/s003359900615;
Mucklow S., Gordon S., Crocker P.R.;
"Characterization of the mouse sialoadhesin gene, Sn.";
Mamm. Genome 8:934-937(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
CHARACTERIZATION.
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=2050106;
Crocker P.R.;
"Purification and properties of sialoadhesin, a sialic acid-binding
receptor of murine tissue macrophages.";
EMBO J. 10:1661-1669(1991).
[5]
SIALIC ACID-BINDING.
PubMed=7533044; DOI=10.1016/S0960-9822(00)00220-7;
Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E.,
Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.;
"Sialoadhesin, myelin-associated glycoprotein and CD22 define a new
family of sialic acid-dependent adhesion molecules of the
immunoglobulin superfamily.";
Curr. Biol. 4:965-972(1994).
[6]
INTERACTION WITH SPN.
PubMed=11238599; DOI=10.4049/jimmunol.166.6.3637;
van den Berg T.K., Nath D., Ziltener H.J., Vestweber D., Fukuda M.,
van Die I., Crocker P.R.;
"CD43 functions as a T cell counterreceptor for the macrophage
adhesion receptor sialoadhesin (Siglec-1).";
J. Immunol. 166:3637-3640(2001).
[7]
FUNCTION, INTERACTION WITH CLEC10A, AND TISSUE SPECIFICITY.
PubMed=15364954; DOI=10.1074/jbc.M409300200;
Kumamoto Y., Higashi N., Denda-Nagai K., Tsuiji M., Sato K.,
Crocker P.R., Irimura T.;
"Identification of sialoadhesin as a dominant lymph node counter-
receptor for mouse macrophage galactose-type C-type lectin 1.";
J. Biol. Chem. 279:49274-49280(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Liver, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 20-138 IN COMPLEX WITH
3'SIALYLLACTOSE, AND DISULFIDE BOND.
PubMed=9660955; DOI=10.1016/S1097-2765(00)80071-4;
May A.P., Robinson R.C., Vinson M., Crocker P.R., Jones E.Y.;
"Crystal structure of the N-terminal domain of sialoadhesin in complex
with 3' sialyllactose at 1.85 A resolution.";
Mol. Cell 1:719-728(1998).
[10]
STRUCTURE BY NMR OF 20-138, AND MUTAGENESIS OF TRP-21 AND ARG-116.
PubMed=10393093; DOI=10.1042/bj3410355;
Crocker P.R., Vinson M., Kelm S., Drickamer K.;
"Molecular analysis of sialoside binding to sialoadhesin by NMR and
site-directed mutagenesis.";
Biochem. J. 341:355-361(1999).
[11]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-138 IN COMPLEX WITH SIALIC
ACID-BASED INHIBITORS, AND DISULFIDE BOND.
PubMed=12737821; DOI=10.1016/S0969-2126(03)00073-X;
Zaccai N.R., Maenaka K., Maenaka T., Crocker P.R., Brossmer R.,
Kelm S., Jones E.Y.;
"Structure-guided design of sialic acid-based Siglec inhibitors and
crystallographic analysis in complex with sialoadhesin.";
Structure 11:557-567(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-137 IN COMPLEX WITH SIALIC
ACID-CONTAINING PEPTIDE, AND DISULFIDE BOND.
PubMed=15488769; DOI=10.1016/j.bbapap.2004.08.015;
Bukrinsky J.T., St Hilaire P.M., Meldal M., Crocker P.R.,
Henriksen A.;
"Complex of sialoadhesin with a glycopeptide ligand.";
Biochim. Biophys. Acta 1702:173-179(2004).
-!- FUNCTION: Acts as an endocytic receptor mediating clathrin
dependent endocytosis. Macrophage-restricted adhesion molecule
that mediates sialic-acid dependent binding to lymphocytes,
including granulocytes, monocytes, natural killer cells, B-cells
and CD8 T-cells (By similarity). Preferentially binds to alpha-
2,3-linked sialic acid. Binds to SPN/CD43 on T-cells. May play a
role in hematopoiesis. May act as a counter-receptor for CLEC10A
in lymph node. {ECO:0000250, ECO:0000269|PubMed:15364954}.
-!- SUBUNIT: Interacts with CLEC10A. {ECO:0000269|PubMed:11238599,
ECO:0000269|PubMed:12737821, ECO:0000269|PubMed:15364954,
ECO:0000269|PubMed:15488769, ECO:0000269|PubMed:9660955}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q62230-1; Sequence=Displayed;
Name=2;
IsoId=Q62230-2; Sequence=VSP_002573, VSP_002574;
Name=3;
IsoId=Q62230-3; Sequence=VSP_002575, VSP_002576;
-!- TISSUE SPECIFICITY: Detected in lymph node in the subcapsular
sinus, interfollicular regions, and T and B-cell boundary (at
protein level). Expressed by macrophages in various tissues.
Highest expression in spleen and lymph node with lower amounts in
lung, liver, bone marrow, heart and skin. No expression in thymus,
kidney, brain or small intestine. {ECO:0000269|PubMed:15364954}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC
(sialic acid binding Ig-like lectin) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA85268.1; Type=Frameshift; Positions=895, 897, 900; Evidence={ECO:0000305};
Sequence=CAA85290.1; Type=Frameshift; Positions=895, 897, 900; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Siglec-1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_193";
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EMBL; Z36293; CAA85290.1; ALT_FRAME; mRNA.
EMBL; Z36233; CAA85268.1; ALT_FRAME; mRNA.
EMBL; Z36234; CAA85269.1; -; mRNA.
EMBL; U92842; AAB95641.1; -; Genomic_DNA.
EMBL; U92833; AAB95641.1; JOINED; Genomic_DNA.
EMBL; U92834; AAB95641.1; JOINED; Genomic_DNA.
EMBL; U92836; AAB95641.1; JOINED; Genomic_DNA.
EMBL; U92837; AAB95641.1; JOINED; Genomic_DNA.
EMBL; U92838; AAB95641.1; JOINED; Genomic_DNA.
EMBL; U92839; AAB95641.1; JOINED; Genomic_DNA.
EMBL; U92840; AAB95641.1; JOINED; Genomic_DNA.
EMBL; U92841; AAB95641.1; JOINED; Genomic_DNA.
EMBL; AL831736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL833771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; S50065; S50065.
RefSeq; NP_035556.3; NM_011426.3.
UniGene; Mm.1374; -.
PDB; 1OD7; X-ray; 3.00 A; A=20-138.
PDB; 1OD9; X-ray; 2.10 A; A=20-138.
PDB; 1ODA; X-ray; 3.31 A; A=20-138.
PDB; 1QFO; X-ray; 1.85 A; A/B/C=20-138.
PDB; 1QFP; X-ray; 2.80 A; A=20-138.
PDB; 1URL; X-ray; 2.40 A; A=20-137.
PDB; 2BVE; X-ray; 2.20 A; A/B=20-138.
PDBsum; 1OD7; -.
PDBsum; 1OD9; -.
PDBsum; 1ODA; -.
PDBsum; 1QFO; -.
PDBsum; 1QFP; -.
PDBsum; 1URL; -.
PDBsum; 2BVE; -.
ProteinModelPortal; Q62230; -.
SMR; Q62230; -.
BioGrid; 203360; 1.
IntAct; Q62230; 2.
MINT; MINT-4135133; -.
STRING; 10090.ENSMUSP00000028794; -.
iPTMnet; Q62230; -.
PhosphoSitePlus; Q62230; -.
PaxDb; Q62230; -.
PRIDE; Q62230; -.
GeneID; 20612; -.
KEGG; mmu:20612; -.
UCSC; uc008mkp.1; mouse. [Q62230-3]
UCSC; uc008mkq.1; mouse. [Q62230-2]
CTD; 6614; -.
MGI; MGI:99668; Siglec1.
eggNOG; ENOG410KDW5; Eukaryota.
eggNOG; ENOG410ZJZH; LUCA.
HOGENOM; HOG000154365; -.
HOVERGEN; HBG003550; -.
InParanoid; Q62230; -.
KO; K06548; -.
EvolutionaryTrace; Q62230; -.
PRO; PR:Q62230; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0070234; P:positive regulation of T cell apoptotic process; IMP:MGI.
Gene3D; 2.60.40.10; -; 20.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07679; I-set; 3.
Pfam; PF00047; ig; 1.
Pfam; PF13895; Ig_2; 6.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 16.
SMART; SM00408; IGc2; 15.
SUPFAM; SSF48726; SSF48726; 17.
PROSITE; PS50835; IG_LIKE; 14.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endocytosis; Glycoprotein; Immunoglobulin domain; Lectin; Membrane;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19
CHAIN 20 1695 Sialoadhesin.
/FTId=PRO_0000014969.
TOPO_DOM 20 1639 Extracellular. {ECO:0000255}.
TRANSMEM 1640 1660 Helical. {ECO:0000255}.
TOPO_DOM 1661 1695 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 136 Ig-like V-type.
DOMAIN 153 235 Ig-like C2-type 1.
DOMAIN 239 321 Ig-like C2-type 2.
DOMAIN 326 406 Ig-like C2-type 3.
DOMAIN 416 508 Ig-like C2-type 4.
DOMAIN 509 594 Ig-like C2-type 5.
DOMAIN 602 701 Ig-like C2-type 6.
DOMAIN 704 781 Ig-like C2-type 7.
DOMAIN 795 890 Ig-like C2-type 8.
DOMAIN 894 973 Ig-like C2-type 9.
DOMAIN 980 1079 Ig-like C2-type 10.
DOMAIN 1081 1161 Ig-like C2-type 11.
DOMAIN 1172 1264 Ig-like C2-type 12.
DOMAIN 1245 1337 Ig-like C2-type 13.
DOMAIN 1342 1439 Ig-like C2-type 14.
DOMAIN 1442 1520 Ig-like C2-type 15.
DOMAIN 1534 1627 Ig-like C2-type 16.
REGION 122 126 Sialic acid binding.
MOTIF 827 829 Cell attachment site. {ECO:0000255}.
BINDING 63 63 Sialic acid.
{ECO:0000305|PubMed:9660955}.
BINDING 116 116 Sialic acid.
{ECO:0000305|PubMed:10393093,
ECO:0000305|PubMed:12737821,
ECO:0000305|PubMed:15488769,
ECO:0000305|PubMed:9660955}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 500 500 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 583 583 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 693 693 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 722 722 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 737 737 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 882 882 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1090 1090 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1100 1100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1247 1247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1460 1460 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1474 1474 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 166 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 41 98 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:15488769}.
DISULFID 160 218 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 263 306 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 347 391 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 434 492 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 532 576 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 625 685 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 725 770 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 813 872 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 912 956 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1001 1063 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1103 1145 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1189 1237 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1277 1320 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1363 1422 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1463 1509 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 1552 1611 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 326 340 MAEVKMNPAGPVLEN -> SESWMRLRGPVSGKH (in
isoform 2). {ECO:0000303|PubMed:7925291}.
/FTId=VSP_002573.
VAR_SEQ 341 1695 Missing (in isoform 2).
{ECO:0000303|PubMed:7925291}.
/FTId=VSP_002574.
VAR_SEQ 1529 1599 YPPKTPTLIVFVEPQGGHQGILDCRVDSEPLAILTLHRGSQ
LVASNQLHDAPTKPHIRVTAPPNALRVDIE -> CEYEPIS
ALCLSLHLTGPYQAFSSAQSKGFIGKGLRTLASSLAGCMWF
VSMLGYPALKWRILLPFWDEYRR (in isoform 3).
{ECO:0000303|PubMed:7925291}.
/FTId=VSP_002575.
VAR_SEQ 1600 1695 Missing (in isoform 3).
{ECO:0000303|PubMed:7925291}.
/FTId=VSP_002576.
MUTAGEN 21 21 W->Q: Loss of sialic acid binding.
{ECO:0000269|PubMed:10393093}.
MUTAGEN 116 116 R->A: Loss of sialic acid binding.
{ECO:0000269|PubMed:10393093}.
MUTAGEN 116 116 R->L: 10-fold loss in affinity to sialic
acid. {ECO:0000269|PubMed:10393093}.
CONFLICT 159 159 N -> F (in Ref. 2; AAB95641).
{ECO:0000305}.
CONFLICT 197 197 V -> S (in Ref. 1; CAA85268/CAA85290 and
2; AAB95641). {ECO:0000305}.
CONFLICT 590 590 P -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 727 727 V -> G (in Ref. 1; CAA85268/CAA85290 and
2; AAB95641). {ECO:0000305}.
CONFLICT 759 760 PV -> LL (in Ref. 1; CAA85268/CAA85290
and 2; AAB95641). {ECO:0000305}.
CONFLICT 1050 1052 IHF -> FLV (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1055 1056 LE -> VQ (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1062 1062 T -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1066 1066 S -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1426 1426 N -> H (in Ref. 1; CAA85268/CAA85290 and
2; AAB95641). {ECO:0000305}.
CONFLICT 1453 1453 V -> W (in Ref. 1; CAA85268/CAA85290 and
2; AAB95641). {ECO:0000305}.
STRAND 22 24 {ECO:0000244|PDB:1QFO}.
STRAND 27 32 {ECO:0000244|PDB:1QFO}.
STRAND 37 39 {ECO:0000244|PDB:1QFO}.
STRAND 42 44 {ECO:0000244|PDB:1QFO}.
STRAND 56 62 {ECO:0000244|PDB:1QFO}.
TURN 63 66 {ECO:0000244|PDB:1QFO}.
STRAND 68 74 {ECO:0000244|PDB:1QFO}.
HELIX 76 78 {ECO:0000244|PDB:1QFO}.
TURN 81 86 {ECO:0000244|PDB:1QFO}.
STRAND 87 89 {ECO:0000244|PDB:1QFO}.
HELIX 93 95 {ECO:0000244|PDB:1QFO}.
STRAND 100 102 {ECO:0000244|PDB:1QFO}.
HELIX 107 109 {ECO:0000244|PDB:1QFO}.
STRAND 111 118 {ECO:0000244|PDB:1QFO}.
STRAND 124 126 {ECO:0000244|PDB:1QFO}.
STRAND 131 136 {ECO:0000244|PDB:1QFO}.
SEQUENCE 1695 AA; 182979 MW; AF704F68C40E113A CRC64;
MCVLFSLLLL ASVFSLGQTT WGVSSPKNVQ GLSGSCLLIP CIFSYPADVP VSNGITAIWY
YDYSGKRQVV IHSGDPKLVD KRFRGRAELM GNMDHKVCNL LLKDLKPEDS GTYNFRFEIS
DSNRWLDVKG TTVTVTTDPS PPTITIPEEL REGMERNFNC STPYLCLQEK QVSLQWRGQD
PTHSVTSSFQ SLEPTGVYHQ TTLHMALSWQ DHGRTLLCQF SLGAHSSRKE VYLQVPHAPK
GVEILLSSSG RNILPGDPVT LTCRVNSSYP AVSAVQWARD GVNLGVTGHV LRLFSAAWND
SGAYTCQATN DMGSLVSSPL SLHVFMAEVK MNPAGPVLEN ETVTLLCSTP KEAPQELRYS
WYKNHILLED AHASTLHLPA VTRADTGFYF CEVQNAQGSE RSSPLSVVVR YPPLTPDLTT
FLETQAGLVG ILHCSVVSEP LATVVLSHGG LTLASNSGEN DFNPRFRISS APNSLRLEIR
DLQPADSGEY TCLAVNSLGN STSSLDFYAN VARLLINPSA EVVEGQAVTL SCRSGLSPAP
DTRFSWYLNG ALLLEGSSSS LLLPAASSTD AGSYYCRTQA GPNTSGPSLP TVLTVFYPPR
KPTFTARLDL DTSGVGDGRR GILLCHVDSD PPAQLRLLHK GHVVATSLPS RCGSCSQRTK
VSRTSNSLHV EIQKPVLEDE GVYLCEASNT LGNSSAAASF NAKATVLVIT PSNTLREGTE
ANLTCNVNQE VAVSPANFSW FRNGVLWTQG SLETVRLQPV ARTDAAVYAC RLLTEDGAQL
SAPVVLSVLY APDPPKLSAL LDVGQGHMAV FICTVDSYPL AHLSLFRGDH LLATNLEPQR
PSHGRIQAKA TANSLQLEVR ELGLVDSGNY HCEATNILGS ANSSLFFQVR GAWVQVSPSP
ELREGQAVVL SCQVPTGVSE GTSYSWYQDG RPLQESTSST LRIAAISLRQ AGAYHCQAQA
PDTAIASLAA PVSLHVSYTP RHVTLSALLS TDPERLGHLV CSVQSDPPAQ LQLFHRNRLV
ASTLQGADEL AGSNPRLHVT VLPNELRLQI HFPELEDDGT YTCEASNTLG QASAAADFDA
QAVRVTVWPN ATVQEGQQVN LTCLVWSTHQ DSLSYTWYKG GQQLLGARSI TLPSVKVLDA
TSYRCGVGLP GHAPHLSRPV TLDVLHAPRN LRLTYLLETQ GRQLALVLCT VDSRPPAQLT
LSHGDQLVAS STEASVPNTL RLELQDPRPS NEGLYSCSAH SPLGKANTSL ELLLEGVRVK
MNPSGSVPEG EPVTVTCEDP AALSSALYAW FHNGHWLQEG PASSLQFLVT TRAHAGAYFC
QVHDTQGTRS SRPASLQILY APRDAVLSSF RDSRTRLMVV IQCTVDSEPP AEMVLSHNGK
VLAASHERHS SASGIGHIQV ARNALRLQVQ DVTLGDGNTY VCTAQNTLGS ISTTQRLLTE
TDIRVTAEPG LDVPEGTALN LSCLLPGGSG PTGNSSFTWF WNRHRLHSAP VPTLSFTPVV
RAQAGLYHCR ADLPTGATTS APVMLRVLYP PKTPTLIVFV EPQGGHQGIL DCRVDSEPLA
ILTLHRGSQL VASNQLHDAP TKPHIRVTAP PNALRVDIEE LGPSNQGEYV CTASNTLGSA
SASAYFGTRA LHQLQLFQRL LWVLGFLAGF LCLLLGLVAY HTWRKKSSTK LNEDENSAEM
ATKKNTIQEE VVAAL


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EIAAB38914 Homo sapiens,Human,Sialic acid-binding Ig-like lectin 1,Sialoadhesin,SIGLEC1,Siglec-1,SN
EIAAB38451 MIS,Mouse,mSiglec-E,Mus musculus,Myeloid inhibitory siglec,Sialic acid-binding Ig-like lectin 12,Sialic acid-binding Ig-like lectin 5,Sialic acid-binding Ig-like lectin E,Sialic acid-binding Ig-like l
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EIAAB38460 Mouse,mSiglec-F,Mus musculus,Sialic acid-binding Ig-like lectin 5,Sialic acid-binding Ig-like lectin F,Siglec5,Siglec-5,Siglecf,Siglec-F
EIAAB38463 CDw329,Homo sapiens,Human,SAF2,SAF-2,Sialic acid-binding Ig-like lectin 8,Sialoadhesin family member 2,SIGLEC8,Siglec-8
EIAAB38450 Homo sapiens,Human,Sialic acid-binding Ig-like lectin 11,Sialic acid-binding lectin 11,SIGLEC11,Siglec-11,UNQ9222_PRO28718
EIAAB38462 Adhesion inhibitory receptor molecule 1,AIRM1,AIRM-1,CDw328,D-siglec,Homo sapiens,Human,p75,QA79 membrane protein,Sialic acid-binding Ig-like lectin 7,SIGLEC7,Siglec-7
EIAAB38455 Homo sapiens,Human,Sialic acid-binding Ig-like lectin 16,SIGLEC16,Siglec-16,SIGLECP16,Siglec-P16
EIAAB38449 Homo sapiens,Human,Sialic acid-binding Ig-like lectin 10,SIGLEC10,Siglec-10,Siglec-like protein 2,SLG2,UNQ477_PRO940
EIAAB38454 CD33 antigen-like 3,CD33L3,Homo sapiens,Human,Sialic acid-binding Ig-like lectin 15,SIGLEC15,Siglec-15
EIAAB38461 CD33 antigen-like 1,CD33L,CD33L1,CDw327,Homo sapiens,Human,OBBP1,OB-BP1,Obesity-binding protein 1,Sialic acid-binding Ig-like lectin 6,SIGLEC6,Siglec-6
EIAAB38459 CD33 antigen-like 2,CD33L2,Homo sapiens,Human,OB-binding protein 2,OBBP2,OB-BP2,Obesity-binding protein 2,Sialic acid-binding Ig-like lectin 5,SIGLEC5,Siglec-5
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U1513m CLIA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,Cd22,Lyb-8,Mouse,Mus musculus,Sialic acid-binding Ig-like lectin 2,Siglec2,Siglec-2,T-cell surface antigen Leu-14 96T
E1513h ELISA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,CD22,Homo sapiens,Human,Sialic acid-binding Ig-like lectin 2,SIGLEC2,Siglec-2,T-cell surface antigen Leu-14 96T
E1513h ELISA kit B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,CD22,Homo sapiens,Human,Sialic acid-binding Ig-like lectin 2,SIGLEC2,Siglec-2,T-cell surface antigen Leu-14 96T
U1513h CLIA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,CD22,Homo sapiens,Human,Sialic acid-binding Ig-like lectin 2,SIGLEC2,Siglec-2,T-cell surface antigen Leu-14 96T
EIAAB06320 Cd33,Mouse,Mus musculus,Myeloid cell surface antigen CD33,Sialic acid-binding Ig-like lectin 3,Siglec3,Siglec-3
EIAAB06319 CD33,gp67,Homo sapiens,Human,Myeloid cell surface antigen CD33,Sialic acid-binding Ig-like lectin 3,SIGLEC3,Siglec-3
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