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ELISA Kit for Human Sialic acid-binding Ig-like lectin 7

SKU : BHE13809963

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E15137h
Alternative Names	Adhesion inhibitory receptor molecule 1 ; AIRM-1 ; CDw328 ; D-siglec ; QA79 membrane protein ; p75 ; CD328 ; AIRM1
Categories	Elisa
Function	Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro).
Specificity	Natural and recombinant Human Sialic acid-binding Ig-like lectin 7
Subcellular Location	Membrane Single-pass type I membrane protein
Detection Range	0.156-10ng/ml
Entryname	SIGL7_HUMAN
Method Type	Sandwich
Platform	PF07686
Protein Name	Sialic acid-binding Ig-like lectin 7
Sensitivity	0.078ng/mL
Sequence	50: MLLLLLLPLL ; WGRERVEGQK ; SNRKDYSLTM ; QSSVTVQEGM ; CVHVRCSFSY ; 100: PVDSQTDSDP ; VHGYWFRAGN ; DISWKAPVAT ; NNPAWAVQEE ; TRDRFHLLGD ; 150: PQTKNCTLSI ; RDARMSDAGR ; YFFRMEKGNI ; KWNYKYDQLS ; VNVTALTHRP ; 200: NILIPGTLES ; GCFQNLTCSV ; PWACEQGTPP ; MISWMGTSVS ; PLHPSTTRSS ; 250: VLTLIPQPQH ; HGTSLTCQVT ; LPGAGVTTNR ; TIQLNVSYPP ; QNLTVTVFQG ; 300: EGTASTALGN ; SSSLSVLEGQ ; SLRLVCAVDS ; NPPARLSWTW ; RSLTLYPSQP ; 350: SNPLVLELQV ; HLGDEGEFTC ; RAQNSLGSQH ; VSLNLSLQQE ; YTGKMRPVSG ; 400: VLLGAVGGAG ; ATALVFLSFC ; VIFIVVRSCR ; KKSARPAADV ; GDIGMKDANT ; 450: IRGSASQGNL ; TESWADDNPR ; HHGLAAHSSG ; EEREIQYAPL ; SFHKGEPQDL ; 467: SGQEATNNEY ; SEIKIPK
Sequence Length	467
String	Q9Y286
Sub Unit	Interacts with PTPN6/SHP-1 upon phosphorylation.

Uniprot	Q9Y286
Gene Name	SIGLEC7
Immunogen Species	Homo Sapiens (Human)
Kegg	hsa:27036
Unigene	Hs.655393

Reference	1. "Identification and characterization of a novel siglec, siglec-7, expressed by human natural killer cells and monocytes." Nicoll G., Ni J., Liu D., Klenerman P., Munday J., Dubock S., Mattei M.-G., Crocker P.R. J. Biol. Chem.274:34089-34095(1999) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) tissue: Dendritic cell. 2. "Identification and molecular cloning of p75/AIRM1, a novel member of the sialoadhesin family that functions as an inhibitory receptor in human natural killer cells." Falco M., Biassoni R., Bottino C., Vitale M., Sivori S., Augugliaro R., Moretta L., Moretta A. J. Exp. Med.190:793-802(1999) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4);PHOSPHORYLATION;INTERACTION WITH PTPN6 tissue: Lymphoid tissue. 3. "Characterization of a novel siglec from dendritic cells." Zhang W., Wan T., Cao X. Submitted (1999-08) to the EMBL/GenBank/DDBJ databases [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) tissue: Dendritic cell. 4. "Siglec-7: a sialic acid-binding lectin of the immunoglobulin superfamily." Angata T., Varki A. Glycobiology10:431-438(2000) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) 5. "Engagement of p75/AIRM1 or CD33 inhibits the proliferation of normal or leukemic myeloid cells." Vitale C., Romagnani C., Falco M., Ponte M., Vitale M., Moretta A., Bacigalupo A., Moretta L., Mingari M.C. Proc. Natl. Acad. Sci. U.S.A.96:15091-15096(1999) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION 6. "Binding specificity of siglec7 to disialogangliosides of renal cell carcinoma: possible role of disialogangliosides in tumor progression." Ito A., Handa K., Withers D.A., Satoh M., Hakomori S. FEBS Lett.498:116-120(2001) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DISIALOGANGLIOSIDE-BINDING 7. "High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family." Alphey M.S., Attrill H., Crocker P.R., van Aalten D.M. J. Biol. Chem.278:3372-3377(2003) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-144;DISULFIDE BOND 8. "Structure of the saccharide-binding domain of the human natural killer cell inhibitory receptor p75/AIRM1." Dimasi N., Moretta A., Moretta L., Biassoni R., Mariuzza R.A. Acta Crystallogr. D60:401-403(2004) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-150;DISULFIDE BOND 9. "The structure of siglec-7 in complex with sialosides: leads for rational structure-based inhibitor design." Attrill H., Takazawa H., Witt S., Kelm S., Isecke R., Brossmer R., Ando T., Ishida H., Kiso M., Crocker P.R., van Aalten D.M. Biochem. J.397:271-278(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-144 IN COMPLEX WITH SIALYLATED LIGAND;GLYCOSYLATION AT ASN-105;DISULFIDE BOND 10. "Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b." Attrill H., Imamura A., Sharma R.S., Kiso M., Crocker P.R., van Aalten D.M. J. Biol. Chem.281:32774-32783(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 18-144 IN COMPLEX WITH ALPHA(2,8)-DISIALYLATED LIGAND GT1B;GLYCOSYLATION AT ASN-105;DISULFIDE BOND 11. "The consensus coding sequences of human breast and colorectal cancers." 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.more... Science314:268-274(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-215

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