Secreted Ectodomain of Sialic Acid-Binding Ig-like Lectin-9 and Monocyte Chemoattractant Protein-1 Promote Recovery after Rat Spinal Cord Injury by Altering Macrophage PolaritySecreted Ectodomain of Sialic Acid-Binding Ig-like Lectin-9 and Monocyte Chemoattractant Protein-1 Promote Recovery after Rat Spinal Cord Injury by Altering Macrophage Polarity ...

Sialic acid-binding Ig-like lectin-7 (Siglec-7) expression is strongly reduced on natural killer (NK) cells from HIV-1 infected viremic patients. To investigate the mechanism(s) underlying this phenomenon, we hypothesized that Siglec-7 could contribute to the infection of CD4pos target cells following its interaction with HIV-1 envelope (Env) glycoprotein 120 (gp120). The ability of Siglec-7 to bind gp120 Env in a sialic acid-dependent manner facilitates the infection of both T cells and monocyte-derived macrophages (MDMs). Indeed, pre-incubation of HIV-1 with soluble Siglec-7 (sSiglec-7) increases the infection rate of CD4pos T cells, which do not constitutively express Siglec-7. Conversely, selective blockade of Siglec-7 markedly reduces the degree of HIV-1 infection in Siglec-7pos MDMs. Finally, the sSiglec-7 amount is increased in the serum of AIDS patients with high levels of HIV-1 viremia and inversely correlates with CD4pos T cell counts. Our results show that Siglec-7 binds HIV-1 and contributes

Sialic-acid-binding immunoglobulin-like lectins (Siglecs) are members of the Ig superfamily that bind sialic acids in different linkages in a wide variety of glycoconjugates. These membrane receptors are expressed in a highly specific manner, predominantly within the haematopoietic system. The CD33- …

First-generation immune checkpoint inhibitors, including anti-CTLA-4 and anti-programmed death 1 (anti-PD-1) antibodies, have led to major clinical progress, yet resistance frequently leads to treatment failure. Thus, new targets acting on T cells are needed. CD33-related sialic acid-binding immunoglobulin-like lectins (Siglecs) are pattern-recognition immune receptors binding to a range of sialoglycan ligands, which appear to function as self-associated molecular patterns (SAMPs) that suppress autoimmune responses. Siglecs are expressed at very low levels on normal T cells, and these receptors were not until recently considered as interesting targets on T cells for cancer immunotherapy. Here, we show an upregulation of Siglecs, including Siglec-9, on tumor-infiltrating T cells from non-small cell lung cancer (NSCLC), colorectal, and ovarian cancer patients. Siglec-9-expressing T cells coexpressed several inhibitory receptors, including PD-1. Targeting of the sialoglycan-SAMP/Siglec pa

First-generation immune checkpoint inhibitors, including anti-CTLA-4 and anti-programmed death 1 (anti-PD-1) antibodies, have led to major clinical progress, yet resistance frequently leads to treatment failure. Thus, new targets acting on T cells are needed. CD33-related sialic acid-binding immunoglobulin-like lectins (Siglecs) are pattern-recognition immune receptors binding to a range of sialoglycan ligands, which appear to function as self-associated molecular patterns (SAMPs) that suppress autoimmune responses. Siglecs are expressed at very low levels on normal T cells, and these receptors were not until recently considered as interesting targets on T cells for cancer immunotherapy. Here, we show an upregulation of Siglecs, including Siglec-9, on tumor-infiltrating T cells from non-small cell lung cancer (NSCLC), colorectal, and ovarian cancer patients. Siglec-9-expressing T cells coexpressed several inhibitory receptors, including PD-1. Targeting of the sialoglycan-SAMP/Siglec pathway in ...

CD22 and sialic acid-binding Ig-like lectin (Siglec)-G are members of the Siglec family of inhibitory coreceptors expressed on B cells that participate in enforcement of peripheral B cell tolerance. We have shown previously that when a BCR engages its cognate Ag on a cell surface that also expresses Siglec ligands, B cell Siglecs are recruited to the immunological synapse, resulting in suppression of BCR signaling and B cell apoptosis. Because all cells display sialic acids, and CD22 and Siglec-G have distinct, yet overlapping, specificities for sialic acid-containing glycan ligands, any cell could, in principle, invoke this tolerogenic mechanism for cell surface Ags ...

Siglec-15 serves as a paradigm for several siglecs, including Siglec-14[1], Siglec-16[2] and Siglec-H[3][4], that contain a basic amino acid within the transmembrane domain[5]. This leads to association of these siglecs with a transmembrane adaptor protein containing an immunoreceptor tyrosine based activation motif (ITAM). Siglec-15 is unusual compared to other siglecs that share this paradigm in two respects. Firstly it can associate with two ITAM containing adaptors, DAP12 and DAP10, whereas Siglec-14, Siglec-16, and Siglec-H show a restricted association with DAP12. Siglec-15 is also unusual in having four cysteine residues in the V-set domain predicted to result in an inter-sheet disulfide that is absent from all other known siglecs. These potentially activating siglecs are expressed on myeloid cells and dendritic cells and may be involved in innate responses to pathogen challenge. ...

Sialic acid binding immunoglobulin-type lectin (Siglec) family are inhibitory receptors with diverse roles in the immune system. Siglec family contains 14 members in human and 9 in murine. Differentially expressed on various white blood cells. Here in this review we are focusing on CD22, also known as Sialic Acid-Binding Ig-Like Lectin 2 (Siglec-2). CD22 gene is located on 19q13.12 and is encoding a 140 kD type I transmembrane glycoprotein on the surface of B cells and is part of the immunoglobulin (Ig) superfamily and has been found only on B cells. CD22 has been shown to play a major role in establishing a baseline level of B-cell inhibition, and thus is a critical determinant of homeostasis in humoral immunity ...

Siglec-H, 0.5 mg. Siglec-H, or sialic acid binding immunoglobulin-like lectin H, is a CD33 related protein expressed specifically by plasmacytoid dendritic cells or pDCs (1, 2).

Clone 1A5 recognizes the CD170 antigen, a single-pass transmembrane protein member of the immunoglobulin superfamily, also known as sialic acid-binding Ig-like lectin 5 (siglec-5). CD170 is expressed on neutrophils, monocytes, dendritic cells, and subsets of tissue macrophages. It contains two tyrosine-based motifs in its cytoplasmic tail implicating signaling functions and forms a 140 kDa dimer on the cell surface. Tyrosine phosphorylation of CD170 leads to recruitment of the tyrosine phosphatases SHP-1 and SHP-2, which in turn efficiently inhibits FcεRI-mediated calcium fluxing and serotonin release. CD170 binds α 2-3- and α 2-6-linked sialic acid as well as glycophorin A, and is involved in cell adhesion. - Österreich

Clone REA393 recognizes the human siglec-5 and siglec-14 antigens, which are both single pass transmembrane protein members of the immunoglobulin superfamily. Siglec-5 is also known as CD170. Siglec-5 has four extracellular Ig-like domains and a cytosolic inhibitory motif. Siglec-14 was discovered with three Ig-like domains and has almost complete sequence identity with siglec-5 at the first two Ig-like domains, shows a glycan binding preference similar to that of siglec-5, and associates with the activating adapter protein DAP12. Siglec-5 is expressed on granulocytes and monocytes as well as on plasmacytoid dendritic cells, monocyte-derived dendritic cells, and macrophages. It is potentially involved in the negative regulation of innate immune responses, and also suggested to be a useful diagnostic and therapeutic marker for acute myelogenous leukemia. Siglec-14 is expressed on granulocytes and B cells. Some individuals lack the expression of siglec-14, while they all express siglec-5. Additional

CD33 is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia ...

Ishida A, Akita K, Mori Y, Tanida S, Toda M, Inoue M, Nakada H. Negative regulation of Toll-like receptor-4 signaling through the binding of glycosylphosphatidylinositol-anchored glycoprotein, CD14, with the sialic acid-binding lectin, CD33 ...

CD33 (gp62 or siglec-3) is a glycosylated transmembrane protein that is a member of the sialic acid-binding immunoglobulin-like lectin (siglec) family. The genomic locus of this protein has been mapped to chromosome 19q13.1-3.5. The function of CD33 is not known, but it may have a role in cell-to-cell adhesion. In maturing granulocytic cells, there is progressive down-regulation of CD33 from the blast stage to mature neutrophils. However, in monocytes and macrophages/histiocytes, strong expression of CD33 is maintained throughout maturation ...

Siglecs (sialic acid-binding lg-like lectins) are mainly expressed in the immune system. Sn (sialoadhesin) (siglec-1), CD22 (siglec-2) and siglec-15 are well ...

SIGLEC H, PerCP-eFluor™ 710, clone: eBio440c, eBioscience™ 100μg; PerCP-eFluor™ 710 SIGLEC H, PerCP-eFluor™ 710, clone: eBio440c,...

Siglec-8 is a lectin specific for 6-sulfo-sLe|sup|x|/sup| and a member of the Ig-superfamily. It is expressed almost exclusively in eosinophils; however, basophils and mast cells can express it to a lower degree. Siglec-8 is a 54 kD transmembranal protein; the extracellular domain has one V-set Ig-

Polyclonal antibody for SIGLEC 4A/MAG detection. Host: Rabbit.Size: 100μg/vial. Tested applications: WB. Reactive species: Human. SIGLEC 4A/MAG information: Molecular Weight: 69069 MW; Subcellular Localization: Membrane; Single-pass type I membrane protei

Polyclonal antibody for Siglec 2/CD22 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. Siglec 2/CD22 information: Molecular Weight: 95348 MW; Subcellular Localization: Cell membrane; Single-pass type I membran

Abcams Siglec 9 ELISA Kit suitable for Cell culture supernatant, Serum, Plasma in human. Reliably quantify 130 pg/ml of Siglec 9.

Siglec-3/CD33 Antibodies available through Novus Biologicals. Browse our Siglec-3/CD33 Antibody catalog backed by our Guarantee+.

View our 55 Siglec-3/CD33 products for your research including Siglec-3/CD33 Primary Antibodies, Proteins and Enzymes, cDNA Clones, and Proteome Profiler Antibody Arrays.

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High-quality Siglec-6 proteins from ACROBiosystems. Various species and tags of Siglec-6 proteins. Minimal Batch-to-Batch Variation. Bulks in stock.

High-quality Siglec-8 proteins from ACROBiosystems. Various species and tags of Siglec-8 proteins. Minimal Batch-to-Batch Variation. Bulks in stock.

Fast delivery of SIGLEC8 knockout Human Cell Lines for the study of gene function. Created by CRISPR/Cas9 genome editing. Includes matched wildtype control.

Cynomolgus Siglec-15, His Tag (SG5-C52H6) is expressed from human 293 cells (HEK293). It contains AA Phe 20 - Thr 263 (Accession # A0A2K5UY47-1).

MDNPQALPLFLLLASLVGILTLRASSGLQQTNFSSAFSSDSKSSSQGLGVEVPSIKPPSWKVPDQFLDSK 1 - 70 ASAGISDSSWFPEALSSNMSGSFWSNVSAEGQDLSPVSPFSETPGSEVFPDISDPQVPAKDPKPSFTVKT 71 - 140 PASNISTQVSHTKLSVEAPDSKFSPDDMDLKLSAQSPESKFSAETHSAASFPQQVGGPLAVLVGTTIRLP 141 - 210 LVPIPNPGPPTSLVVWRRGSKVLAAGGLGPGAPLISLDPAHRDHLRFDQARGVLELASAQLDDAGVYTAE 211 - 280 VIRAGVSQQTHEFTVGVYEPLPQLSVQPKAPETEEGAAELRLRCLGWGPGRGELSWSRDGRALEAAESEG 281 - 350 AETPRMRSEGDQLLIVRPVRSDHARYTCRVRSPFGHREAAADVSVFYGPDPPTITVSSDRDAAPARFVTA 351 - 420 GSNVTLRCAAASRPPADITWSLADPAEAAVPAGSRLLLPAVGPGHAGTYACLAANPRTGRRRRSLLNLTV 421 - 490 ADLPPGAPQCSVEGGPGDRSLRFRCSWPGGAPAASLQFQGLPEGIRAGPVSSVLLAAVPAHPRLSGVPIT 491 - 560 CLARHLVATRTCTVTPEAPREVLLHPLVAETRLGEAEVALEASGCPPPSRASWAREGRPLAPGGGSRLRL 561 - 630 SQDGRKLHIGNFSLDWDLGNYSVLCSGALGAGGDQITLIGPSISSWRLQRARDAAVLTWDVERGALISSF 631 - 700 EIQAWPDGPALGRTSTYRDWVSLLILGPQERSAVVPLPPRNPGTWTFRILPILGGQPGTPSQSRVYRAGP 701 - 770 TLSHGAIAGIVLGSLLGLALLAVLLLLCICCLCRFRGKTPEKKKHPSTLVPVVTPSEKKMHSVTPVEISW 771 - 840 PLDLKVPLEDHSSTRAYQAQTPVQLSL 841 - 867 ...

Title: A Sialic Acid-Specific Lectin from the Mushroom Paecilomyces Japonica that Exhibits Hemagglutination Activity and Cytotoxicity. VOLUME: 11 ISSUE: 6. Author(s):Jee Hun Park, Chang Soo Ryu, Ha Na Kim, Young Jun Na, Hyun Joo Park and HaHyung Kim. Affiliation:Physical Pharmacy Laboratory, College of Pharmacy, Chung-Ang University, 221 Huksuk-dong, Dongjakku, Seoul 156-756, Korea Correspondence To: HaHyung Kim.. Keywords:sialic acid, lectin, mushroom, paecilomyces japonica, hemagglutination, cytotoxicity. Abstract: The mushroom Paecilomyces japonica, grown on the silkworm larvae, has been used in Asia as a nutraceutical, tea, and Chinese medicine. In the present study, a sialic acid-specific lectin has been purified from the mushroom P. japonica using affinity chromatography on a fetuin-agarose column. Electrophoretical analyses indicated that this lectin, designated P. japon ica agglu tinin (PJA), is an acidic protein with a molecular mass of 16 kDa, and has no intermolecular disulfide bonds. ...

Malignant mesothelioma is an aggressive cancer with limited therapeutic options. Sialic acid-binding lectin isolated from Rana catesbeiana oocytes (cSBL) is a multifunctional protein with anti-cancer activity. The effects of pemetrexed, cisplatin, and cSBL were evaluated in mesothelioma and normal mesothelial cell lines. We evaluated cytotoxicity, apoptosis, caspase-3 cleavage and activation, cell proliferation, cell cycle arrest, and levels of cell cycle proteins in H28 cells treated with pemetrexed, cisplatin, and cSBL alone or in combination. Treatment with cSBL alone was cytotoxic to mesothelioma cells. The anti-cancer effect of cSBL was observed in a broader range of cell lines and exhibited greater cancer cell selectivity than pemetrexed or cisplatin. Combination treatment with pemetrexed + cSBL resulted in greater dose-dependent cytotoxicity than pemetrexed + cisplatin, the standard of care in mesothelioma. The synergistic effect of pemetrexed + cSBL was mediated by the cytostatic effect ...

Abstract: Siglecs are a family of sialic acid-recognizing immunoglobulin-like lectins that exhibit multiple human-specific and human-universal differences, including changes in binding specificity (Siglec-5, -7, -9, -11, -12 and 14); changes in expression pattern (Siglec-1, -5, -6, and -11); gene conversion (SIGLEC11); gene deletion (SIGLEC13) and pseudogenization (SIGLEC17). Human-unique pseudogenes of SIGLEC12, SIGLEC14 and SIGLEC16 are also polymorphic within human populations, suggesting ongoing selection on this family of genes. The apparently higher concentration of SIGLEC changes in the human lineage may have been selected by interactions with pathogens binding Siglecs, and/or as compensatory responses to the loss of the sialic acid N-glycolylneuraminic acid (Neu5Gc) in humans. Human-specific Siglec changes of particular interest include expression of Siglec-11 in brain microglia, expression of Siglec-6 on placental trophoblast, suppression of Siglec-5 expression on adaptive immune cells, ...

Sialic acid-binding Ig-like lectin 8 is a protein that in humans is encoded by the SIGLEC8 gene. This gene is located on chromosome 19q13.4, about 330 kb downstream of the SIGLEC9 gene. Within the siglec family of transmembrane proteins, Siglec-8 belongs to the CD33-related siglec subfamily, a subfamily that has undergone rapid evolution. Siglec-8 was first identified by CD33 homology screening of ESTs from a cDNA library generated from a patient diagnosed with idiopathic hypereosinophilic syndrome and was originally termed SAF-2 (sialoadhesin family 2). At the tissue level, Siglec-8 mRNA was found to be most highly expressed in lung, PBMCs, spleen, and kidney. Siglec-8 is expressed by human eosinophils, mast cells, and, to a lesser extent, basophils. It has thus garnered attention as a molecule that is uniquely expressed by immune effector cells involved in asthma and allergy. In both eosinophils and mast cells, Siglec-8 is expressed late in development. Siglec-8 transcript and protein are ...

Sepsis is the most frequent cause of death in hospitalized patients, and severe sepsis is a leading contributory factor to acute respiratory distress syndrome (ARDS). At present, there is no effective treatment for these conditions, and care is primarily supportive. Murine sialic acid-binding immunoglobulin-like lectin-E (Siglec-E) and its human orthologs Siglec-7 and Siglec-9 are immunomodulatory receptors found predominantly on hematopoietic cells. These receptors are important negative regulators of acute inflammatory responses and are potential targets for the treatment of sepsis and ARDS. We describe a Siglec-targeting platform consisting of poly(lactic-co-glycolic acid) nanoparticles decorated with a natural Siglec ligand, di(α2→8) N-acetylneuraminic acid (α2,8 NANA-NP). This nanoparticle induced enhanced oligomerization of the murine Siglec-E receptor on the surface of macrophages, unlike the free α2,8 NANA ligand. Furthermore, treatment of murine macrophages with these nanoparticles ...

Siglecs are type I transmembrane proteins expressed primarily on leukocytes. Among them is Siglec-8, a CD33 subfamily member that is selectively expressed on the cell surface of human eosinophils. Siglec-8 has an intracellular immunoreceptor tyrosine-based inhibitory motif (ITIM) and an immunoreceptor tyrosine-based switch motif (ITSM), putatively responsible for signal transduction. In cytokine-activated eosinophils, Siglec-8 binding causes apoptosis with increased mitochondrial damage and ROS production, but exact signaling mechanisms are unknown. Using a mAb (2C4) against Siglec-8 in combination with small molecule inhibitors, we first examined Siglec-8-mediated apoptosis and ROS production by flow cytometry after 24 hr IL-5 priming (30 ng/mL) of human eosinophils. We observed that 2C4-mediated eosinophil apoptosis was inhibited by PP1 and SU6656 (Src kinase inhibitors), ibrutinib (Btk inhibitor), LY294002 (PI3K inhibitor), GF109203x (PKC inhibitor), and sodium orthovanadate (a protein ...

Malignant transformation of cells is associated with aberrant glycosylation presented on the cell-surface. Commonly observed changes in glycan structures during malignancy encompasses aberrant expression and glycosylation of mucins; abnormal branching of N-glycans; and increased presence of sialic acid on proteins and glycolipids. Accumulating evidence supports the notion that the presence of certain glycan structures correlates with cancer progression by affecting tumor cell invasiveness, ability to disseminate through the blood circulation and to metastasize in distant organs. During metastasis tumor cell-derived glycans enable binding to cells in their microenvironment including endothelium and blood constituents through glycan-binding receptors - lectins. In this review we will discuss current concepts how tumor cell-derived glycans contribute to metastasis with the focus on three types of lectins: siglecs, galectins and selectins. Siglecs are present on virtually all hematopoetic cells and usually

December 2nd, 2013 by Naito-Matsui, Y., Takada, S., Kano, Y., Iyoda, T., Sugai, M., Shimizu, A., Inaba, K., Nitschke, L., Tsubata, T., Oka, S., Kozutsumi, Y., Takematsu, H.. Sialic acids (Sias) are often conjugated to the termini of cellular glycans and are key mediators of cellular recognition. Sias are nine-carbon acidic sugars, and, in vertebrates, the major species are N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), differing in structure at the C5 position. Previously, we described a positive feedback loop involving regulation of Neu5Gc expression in mouse B cells. In this context, Neu5Gc negatively regulated B-cell proliferation and Neu5Gc expression was suppressed upon activation. Similarly, resting mouse T cells expressed principally Neu5Gc, and Neu5Ac was induced upon activation. In the present work, we used various probes to examine sialoglycan expression by activated T cells in terms of the Sia species expressed and the linkages of Sias to glycans. Upon T-cell ...

Human carcinomas can metabolically incorporate and present the dietary non-human sialic acid Neu5Gc, which differs from the human sialic acid N-acetylneuraminic acid (Neu5Ac) by 1 oxygen atom. Tumor-associated Neu5Gc can interact with low levels of circulating anti-Neu5Gc antibodies, thereby facilitating tumor progression via chronic inflammation in a human-like Neu5Gc-deficient mouse model. Here we show that human anti-Neu5Gc antibodies can be affinity-purified in substantial amounts from clinically approved intravenous IgG (IVIG) and used at higher concentrations to suppress growth of the same Neu5Gc-expressing tumors. Hypothesizing that this polyclonal spectrum of human anti-Neu5Gc antibodies also includes potential cancer biomarkers, we then characterize them in cancer and noncancer patients sera, using a novel sialoglycan microarray presenting multiple Neu5Gc-glycans and control Neu5Ac-glycans. Antibodies against Neu5Gcα2-6GalNAcα1-O-Ser/Thr (GcSTn) were found to be more prominent in ...

Video articles in JoVE about sambucus nigra include Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples, Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution, A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples, Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay .

CD170 (Siglec F), clone: 1RNM44N, eBioscience™ 25μg; Unconjugated CD170 (Siglec F), clone: 1RNM44N, eBioscience™ Primary Antibodies CD151 to CD200

VSIG10L2 (V-set and immunoglobulin domain containing 10 like 2), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.

MedChemExpress offers high purity Siglec-15 Protein, Cynomolgus (HEK 293, His) with excellent lot-to-lot consistency, superior biological activity and low endotoxin levels.

R01 AI072265, NIH/NIAID - Bochner (PI). Studies in this grant will explore whether Siglec-8, a molecule selectively expressed by eosinophils and mast cells, can be targeted for both diagnostic and therapeutic purposes in allergic, gastrointestinal and malignant diseases.. Siglecs (sialic acid-binding, immunoglobulin-like lectins) are cell surface proteins found predominantly on leukocytes. Siglec-8 was discovered by us about a decade ago and is selectively expressed on eosinophils and mast cells. Its closest functional paralog in the mouse is Siglec-F, which is also selectively expressed by eosinophils but unfortunately not on mast cells. Both Siglec-8 and Siglec-F preferentially and uniquely recognize the glycan 6-sulfo-sialyl Lewis X (6-sulfo-sLeX) and its non-fucosylated form. Engagement of Siglec-8/-F with antibodies (Abs) and/or artificial ligands causes eosinophil death. Administration of Siglec-F Abs in mouse models of chronic allergic asthma and eosinophilia normalizes eosinophilic ...

Myelin-associated glycoprotein (MAG, Siglec-4) is unique among the siglecs in that it is expressed exclusively on neuronal glial cells[1][2]. It is the most highly conserved among the siglecs in mammalian species. This siglec paradigm is unique in its activity of stabilizing axon-myelin interactions. MAG has a cytoplasmic domain that is devoid of ITIMs, but contains a tyrosine-based motif associated with binding the FYN tyrosine kinase, believed to play a role in its activity in myelin-axon interactions. MAG recognizes as ligands sialoside sequences found on gangliosides that are abundant in axonal membranes[2]. It is one of several proteins in myelin that negatively regulate axon outgrowth following tissue injury, an activity that involves MAG-ligand interactions. Evidence suggests that inhibition of MAG-ligand interactions may enhance neurite outgrowth and repair of injured neurons[3][4][5]. ...

Video articles in JoVE about heart valves include Biaxial Mechanical Characterizations of Atrioventricular Heart Valves, Cardiac Exam III: Abnormal Heart Sounds, Cardiac Exam I: Inspection and Palpation, Echocardiographic Approaches and Protocols for Comprehensive Phenotypic Characterization of Valvular Heart Disease in Mice, Assessing Bacterial Invasion of Cardiac Cells in Culture and Heart Colonization in Infected Mice Using Listeria monocytogenes, Reprogramming Primary Amniotic Fluid and Membrane Cells to Pluripotency in Xeno-free Conditions, Synthesis of Soft Polysiloxane-urea Elastomers for Intraocular Lens Application, Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay , Echocardiographic Assessment of Cardiac Anatomy and Function in Adult Rats, An In Vitro Model of a Parallel-Plate Perfusion System to Study Bacterial Adherence to Graft Tissues, Two Methods for Decellularization of Plant Tissues for Tissue Engineering Applications, Light-sheet

Sialic acid binding immunoglobulin-type lectin (siglec) belongs to the immunoglobulin superfamily (IgSF), which acts as regulator involved in glycan recognition and signal transduction in the immune and nervous systems. In the present study, a siglec gene (designated CgSiglec-1) was characterized from the Pacific oyster, Crassostrea gigas. The cDNA of CgSiglec-1 was of 1251 bp encoding a predicted ...

Meininger, M.; Santos da Silva, F. V.; Cajic, S.; Hennig, R.; Rapp, E.; Zwanziger, F.; Laufer, S.; Wiesmüller, K.-H.; Rotering, H.; Reichl, U. et al.; Wolff, M. W.: Development of a Sialic Acid-Specific Affinity Chromatography for the Purification and Separation of Glycoprotein Isoforms. ISPPP-International Symposium on the Separation of Proteins, Peptides & Polynucleotides, Boston, USA (2013 ...

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TY - JOUR. T1 - Characterization of expression of glycan ligands for Siglec-F in normal mouse lungs. AU - Guo, Jin P.. AU - Brummet, Mary E.. AU - Myers, Allen C.. AU - Na, Ho Jeong. AU - Rowland, Elizabeth. AU - Schnaar, Ronald L.. AU - Zheng, Tao. AU - Zhu, Zhou. AU - Bochner, Bruce S.. PY - 2011/2/1. Y1 - 2011/2/1. N2 - Sialic acid-binding immunoglobulin-like lectin (Siglec)-F, an inhibitory receptor on mouse eosinophils, preferentially recognizes the glycan ligand 69-sulfated sialyl Lewis X, but little is known about the requirements for its lung expression. RT-PCR and immunohistochemistry were used to detect and localize the sulfotransferase keratin sulfate galactose 6-O sulfotransferase (KSGal6ST, alsoknown as carbohydrate sulfotransferase 1; gene name, Chst1) that is putatively required for 6′-sulfated Sialyl Lewis X synthesis. RT-PCR detected the greatest constitutive expression of Chst1 in lung, liver, andspleen tissue.Immunohistochemistry localized the expression of KSGal6ST in lung ...

B-lymphocyte antigen CD22 is a member of the recently described sialoadhesin family of immunoglobulin-like cell-surface glycoproteins that bind glycoconjugates terminating in sialic acid. One prominent ligand for CD22 is the highly glycosylated leukocyte surface protein CD45. Using surface plasmon resonance spectroscopy, we characterized the interaction of recombinant mouse CD22 with native CD45 purified from rat thymus (CD45-thy). By in situ desialylation and resialylation of immobilized CD45-thy, we show that mouse CD22 binds to the sialoglycoconjugate NeuGc alpha 2-6Gal beta 1-4GlcNAc carried on CD45-thy N-glycans. Previous studies have shown that the sialic acid-binding site lies within the two membrane-distal domains of CD22 (domains 1 and 2), which are V-set and C2-set immunoglobulin superfamily domains, respectively. To further localize the binding site, we have made 42 single amino acid substitutions throughout both domains. All 12 mutations that abrogated binding to CD45-thy without disrupting

Compare sialic acid binding Ig like lectin 11 Biomolecules from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.

Build: Wed Jun 21 18:33:50 EDT 2017 (commit: 4a3b2dc). National Center for Advancing Translational Sciences (NCATS), 6701 Democracy Boulevard, Bethesda MD 20892-4874 • 301-435-0888. ...

Expression of CD22 (SIGLEC-2, SIGLEC2) in cancer tissue. The cancer tissue page shows antibody staining of the protein in 20 different cancers.

Mouse Monoclonal Anti-Siglec-3/CD33 Antibody (44M12D3) [DyLight 405]. Validated: WB, IHC, IHC-P. Tested Reactivity: Human. 100% Guaranteed.