Tetraspanins are a superfamily of glycoproteins that function as organisers of membranes by clustering with each other to form tetraspanin-enriched microdomains, into which certain other receptors and signalling proteins are recruited and regulated. Tetraspanin microdomains have been implicated in a range of biological processes including cell signalling, adhesion, intracellular trafficking, cell-cell fusion and viral entry. The tetraspanin CD37 was recently shown to negatively regulate the C-type lectin-like receptor dectin-1, which is essential for innate immune responses to fungal pathogens. The aim of this thesis was to firstly develop a cell line model system to investigate the mechanism by which tetraspanins inhibit dectin-1, and to secondly extend this work to the dectin-1-related CLEC-2, which is essential for platelet thrombus formation and stability. Using a nuclear factor of activated T-cells (NFAT) transcriptional reporter assay in the Jurkat T-cell line, transient over-expression ...
A number of genes encoding C-type lectin molecules have been mapped to the natural killer gene complex (NKC) at the distal region of mouse chromosome 6 and to a syntenic region on human chromosome 12p12-p13. In addition to those receptors which regulate NK cell function, related structures expressed on other cells types have also been localized to this chromosomal region. Among these are a number of recently characterized genes, including macrophage C-type lectin (MCL), macrophage-inducible C-type lectin (Mincle), dendritic cell immunoreceptor (DCIR) and dendritic cell-associated lectin-2 (Dectin-2). The amino acid sequences comprising the single C-type lectin domains of MCL, Mincle, DCIR and Dectin-2 are shown here to be closely related to each other. These molecules show overall similarity to two groups of animal C-type lectins, groups II and V, which demonstrate type II transmembrane topology. In this study, sequence analysis suggests that MCL, Mincle, DCIR and Dectin-2 represent a subset of group II
Clone REA431 recognizes CD371, the human C-type lectin domain family 12 member A (CLEC12A) antigen, a single-pass type II membrane protein which is also known as C-type lectin-like molecule 1 (CLL-1), dendritic cell-associated lectin 2 (DCAL2), or myeloid inhibitory C-type lectin-like receptor (MICL). CD371 (CLEC12A) is a immunoreceptor tyrosine-based inhibitory motif (ITIM) containing C-type lectin receptor encoded within the dectin-1 cluster. This receptor binds unknown endogenous ligands and is widely expressed on innate immune cells, including neutrophils, monocytes, macrophages, and dendritic cells (DCs). There are conflicting data on its expression on human natural killer (NK) cells. Its intracellular ITIM sequence recruits the tyrosine phosphatases SHP-1 and SHP-2 to negatively regulate Syk signaling. Because the expression of CD371 (CLEC12A) can be downregulated under inflammatory conditions, this receptor might be involved in the control of myeloid cell activation. CD371 (CLEC12A) has been
Antigen uptake and processing by innate immune cells is crucial to initiate the immune response. Therein, the endocytic C-type lectin receptors serve as pattern recognition receptors, detecting pathogens by their glycan structures. Herein, we studied the carbohydrate recognition domain of Langerin, a C-type lectin receptor involved in the host defense against viruses such as HIV and influenza as well as bacteria and fungi. Using a combination of nuclear magnetic resonance and molecular dynamics simulations, we unraveled the molecular determinants underlying cargo capture and release encoded in the receptor architecture. Our findings revealed receptor dynamics over several time scales associated with binding and release of the essential cofactor Ca(2+) controlled by the coupled motions of two loops. Applying mutual information theory and site-directed mutagenesis, we identified an allosteric intradomain network that modulates the Ca(2+) affinity depending on the pH, thereby promoting fast ligand ...
Macrophages act as the primary effector cells during Leishmania infection through production of reactive oxygen species (ROS) and interleukin-1 beta (IL-1 beta). However, how macrophage-killing mechanisms are activated during Leishmania-macrophage interactions is poorly understood. Here, we report that the macrophage response against Leishmania infantum in vivo is characterized by an M2b-like phenotype and C-type lectin receptors (CLRs) signature composed of Dectin-1, mannose receptor (MR), and the DC-SIGN homolog SIGNR3 expression. Dectin-1 and MR were crucial for the microbicidal response as indicated by the fact that they activated Syk-p47phox and arachidonic acid (AA)-NADPH oxidase signaling pathways, respectively, needed for ROS production and also triggered Syk-coupled signaling for caspase-1-induced IL-1 beta secretion. In contrast, SIGNR3 has divergent functions during Leishmania infantum pathogenesis; this CLR favored parasite resilience through inhibition of the LTB4-IL-1 beta axis. ...
Natural killer (NK) cells express multiple calcium-dependent (C-type) lectin-like receptors, such as CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), that interact with major histocompatibility complex class I molecules and either inhibit or activate cytotoxicity and cytokine secretion. CLEC2 is a C-type lectin-like receptor expressed in myeloid cells and NK cells (Colonna et al., 2000 [PubMed 10671229]).[supplied by OMIM, Jan 2011 ...
Buy CLEC3B elisa kit, Human C-type lectin domain family 3, member B ELISA Kit-NP_003269.2 (MBS922364) product datasheet at MyBioSource, ELISA Kits
This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. The encoded glycoprotein is a small type II membrane receptor with an extracellular C-type lectin-like domain fold and a cytoplasmic domain with an immunoreceptor tyrosine-based activation motif. It functions as a pattern-recognition receptor that recognizes a variety of beta-1,3-linked and beta-1,6-linked glucans from fungi and plants, and in this way plays a role in innate immune response. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. This gene is closely linked to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. [provided by RefSeq, Jul 2008 ...
Recombinant production and characterization of the carbohydrate recognition domain from Atlantic salmon C-type lectin receptor C (SCLRC)
DC-SIGN recognizes both internal branched mannose residues as well as terminal di-mannoses, α1-3 and α1-4 fucosylated glycan structures and certain N-aceltylglucosamine containing molecules on self proteins and/or pathogens ,ref name=Feinberg 2001/,,ref name=Guo 2004,Guo Y, Feinberg H, Conroy E, Mitchell DA, Alvarez R, Blixt O, Taylor ME, Weis WI and Drickamer K. 2004. Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR. Nat Struct Mol Biol. 11:591-598,/ref,,ref,Mitchell DA, Fadden AJ and Drickamer K. 2001. A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands. J Biol Chem. 276:28939-28945,/ref,,ref name=Liempt 2006,van Liempt E, Bank CM, Mehta P, Garcia-Vallejo JJ, Kawar ZS, Geyer R, Alvarez RA, Cummings RD, Kooyk Y and van Die I. 2006. Specificity of DC-SIGN for mannose- and fucose-containing glycans. FEBS Lett. 580:6123-6131,/ref,,br,,br ...
Dr. Maria Fernandes is the principal investigator on a research project titled "The characterization of MICL, a novel negative regulator of the immune response in arthritis." She and her co-investigator Philippe Tessier, were recently awarded a five year operating grant to support this project. CIHR - IMHA is pleased to profile her work in this issue.. Dr. Fernandes received her PhD in Biochemical Genetics from McGill University before pursing postdoctoral training at Thomas Jefferson University in Philadelphia, Pennsylvania. There, she cloned two novel genes that code for proteins belonging to the C-type lectin family. According to Dr. Fernandes, "C-type lectins play important roles in the immune response. Fascinated by these receptors, I pursued a second post-doctorate in inflammation during which I specialized in myeloid receptor signaling to eventually investigate the role of C-type lectin receptors (CLRs) in the immune system.". Her interest in CLRs and arthritis led her to develop her ...
Clone KVa7-6E7 specifically recognizes mouse dendritic cell-associated C-type lectin 2 (Dectin-2). Dectin-2 is a type II membrane protein and contains a single carbohydrate recognition domain. Like other C-type lectins, mouse Dectin-2 has conserved motifs for the Ca2+ -dependent recognition of mannose. Dectin-2 is located in the natural killer gene complex of chromosome 6. Genomic analyses show that beside a full length Dectin-2 transcript two truncated isoforms are produced by alternative splicing, encoding transmembrane proteins of 168-209 amino acids.¹, ² The expression of Dectin-2 on mouse monocytes and macrophages can be induced by zymosan and thioglycollate.3 Dectin-2 plays a physiological role in antigen presentation and antigen targeting via Dectin-2 can induce a CD8+ T cell response.4 - USA
Adamkiewicz, T.V., McSherry, C., Bach, F.H. et al. Natural killer lectin-like receptors have divergent carboxyl-termini, distinct from C-type lectins. Immunogenetics 39, 218 (1994). https://doi.org/10.1007/BF00241264. Download ...
RecName: Full=C-type lectin domain family 7 member A;AltName: Full=Beta-glucan receptor;AltName: Full=C-type lectin superfamily member 12;AltName: Full=Dendritic cell-associated C-type lectin 1; Short=DC-associated C-type lectin 1; Short=D ...
Transforming growth factor-β (TGF-β) suppresses innate and adaptive immune responses via multiple mechanisms. TGF-β also importantly contributes to the formation of an immunosuppressive tumor microenvironment thereby promoting tumor growth. Amongst others, TGF-β impairs tumor recognition by cytotoxic lymphocytes via NKG2D. NKG2D is a homodimeric C-type lectin-like receptor expressed on virtually all human NK cells and cytotoxic T cells, and stimulates their effector functions upon engagement by NKG2D ligands (NKG2DL). While NKG2DL are mostly absent from healthy cells, their expression is induced by cellular stress and malignant transformation, and, accordingly, frequently detected on various tumor cells. Hence, the NKG2D axis is thought to play a decisive role in cancer immunosurveillance and, obviously, often is compromised in clinically apparent tumors. There is mounting evidence that TGF-β, produced by tumor cells and immune cells in the tumor microenvironment, plays a key role in blunting the
Q6EIG7: C-type lectin domain family 6 member A; C-type lectin superfamily member 10; Dendritic cell-associated C-type lectin 2; DC-associated C-type lectin 2; Dectin- ...
Cell surface receptors are responsible for regulating cellular function on the front line, the cell membrane. Interestingly, accumulating evidence clearly reveals that the members of cell surface receptor families have very similar extracellular ligand-binding regions but opposite signaling systems, either inhibitory or stimulatory. These receptors are designated as paired receptors. Paired receptors often recognize not only physiological ligands but also non-self ligands, such as viral and bacterial products, to fight infections. In this review, we introduce several representative examples of paired receptors, focusing on two major structural superfamilies, the immunoglobulin-like and the C-type lectin-like receptors, and explain how these receptors distinguish self and non-self ligands to maintain homeostasis in the immune system. We further discuss the evolutionary aspects of these receptors as well as the potential drug targets for regulating diseases.
Reagents for the antigen KLRG1 / MAFA / CLEC15A / C-type lectin domain family 15 member A stained with biotin in the Antibody Database
Pattern recognition receptors (PRRs) are crucial for responses to infections and tissue damage; however, their role in autoimmunity is less clear. Herein we demonstrate that 2 C-type lectin receptors (CLRs) Mcl and Mincle play an important role in the pathogenesis of experimental autoimmune encephalomyelitis (EAE), an animal model of multiple sclerosis (MS). Congenic rats expressing lower levels of Mcl and Mincle on myeloid cells exhibited a drastic reduction in EAE incidence. In vivo silencing of Mcl and Mincle or blockade of their endogenous ligand SAP130 revealed that these receptors expression in the central nervous system is crucial for T cell recruitment and reactivation into a pathogenic Th17/GM-CSF phenotype. Consistent with this, we uncovered MCL- and MINCLE-expressing cells in brain lesions of MS patients and we further found an upregulation of the MCL/MINCLE signaling pathway and an increased response following MCL/MINCLE stimulation in peripheral blood mononuclear cells from MS ...
DC-SIGN is a dendritic cell-specific C-type lectin receptor that recognizes highly glycosylated ligands expressed on the surface of various pathogens. This receptor plays an important role in the early stages of many viral infections, including HIV, which makes it an interesting therapeutic target. Glycomimetic compounds are good drug candidates for DC-SIGN inhibition due to their high solubility, resistance to glycosidases, and nontoxicity. We studied the structural properties of the interaction of the tetrameric DC-SIGN extracellular domain (ECD), with two glycomimetic antagonists, a pseudomannobioside (1) and a linear pseudomannotrioside (2). Though the inhibitory potency of 2, as measured by SPR competition experiments, was 1 order of magnitude higher than that of 1, crystal structures of the complexes within the DC-SIGN carbohydrate recognition domain showed the same binding mode for both compounds. Moreover, when conjugated to multivalent scaffolds, the inhibitory potencies of these compounds
The authors wish to add this correction on their paper published in IJMS [1]. Galectin-1 was misclassified as a C-type lectin. Galectin-1 belongs to the family of the S-type lectins, i.e., the galectins. These errors have been amended in an amended version of the manuscript, which is available from the International Journal of Molecular Sciences website. The authors and publisher apologize for the inconvenience. [...]
Antibody Database - Conjugates for the antigen Killer cell lectin-like receptor subfamily A, member 3 / KLRA3 in the Antibody Database
CLEC9A is a group V C-type lectin receptor (CTLR) comprised of a single extracellular C-type lectin domain (CTLD) connected to the transmembrane domain by a stalk region and an intracellular cytoplasmic tail. In humans, CLEC9A is expressed on the cell surface of a subset of Dendritic cells (DCs) and a subset of CD14+CD16- Monocytes.
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Gene Information This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions such as cell adhesion cell-cell signalling glycoprotein turnover and roles in inflammation and immune response. The encoded type 2 transmembrane protein may play a role in inflammatory and immune response. Multiple transcript variants encoding distinct isoforms have been identified for this gene. This gene is closely linked to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. [provided by RefSeq Jul 2008]. ...
Buy our Human DC-SIGN peptide. Ab6092 is a blocking peptide for ab5716 and has been validated in BL. Abcam provides free protocols, tips and expert support for…
CD371 belongs to the C-type lectin family and is expressed on monocytes, macrophages, dendritic cells, granulocytes, and some NK cell subsets.
Reaktivität: Rind (Kuh), Human, Maus and more. 138 verschiedene CLEC6A Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Background Tuberculosis, which is caused by Mycobacterium tuberculosis, remains one of the leading causes of mortality worldwide. The C-type lectin DC-SIGN is known to be the major M. tuberculosis receptor on human ...
DC-SIGN antibody [120507] (CD209 molecule) for FACS, ICC/IF, IHC-P, WB. Anti-DC-SIGN mAb (GTX13487) is tested in Human samples. 100% Ab-Assurance.
PK136 reacts with mouse NK1.1, a transmembrane glycoprotein & C-type lectin receptor expressed on NK cells, and NK-T cells in select mouse strains.
我的實驗室對於闡明病原體引起細胞激素風暴以及致死的分子機轉,和確認預防免疫治療的潛在目標,以預防組織損傷及纖維化。我們從兩個方向探討這些問題:宿主與病原體交互作用以及免疫調節。. Host-Pathogen Interaction. 發炎反應的啟動是經由自然殺手細胞、單核球細胞、巨噬細胞、嗜中性白血球以及血小板上的先天免疫受體受到感染因子、外來抗原或是異常表現的內源性抗原的活化。因此,了解外源性以及內源性抗原在先天免疫反應的分子機轉將能夠開發新的治療策略以治療諸多人類疾病,例如感染症、自體免疫以及過敏反應。我們開發了先天免疫受體陣列(innate immunity receptor array / IIR-EIA)以及C型凝集素受體陣列(C-type lectin receptor array ...
Complete information for CLEC2A gene (Protein Coding), C-Type Lectin Domain Family 2 Member A, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for CLEC10A gene (Protein Coding), C-Type Lectin Domain Containing 10A, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Next-day shipping cDNA ORF clones derived from CLEC11A C-type lectin domain containing 11A available at GenScript, starting from $99.00.
Next-day shipping cDNA ORF clones derived from CLEC11A C-type lectin domain containing 11A available at GenScript, starting from $99.00.
Gene target information for CLEC5A - C-type lectin domain containing 5A (human). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
Dectin-1/CLEC7A Proteins available through Novus Biologicals. Browse our Dectin-1/CLEC7A Protein catalog backed by our Guarantee+.
Rat monoclonal DC-SIGN antibody [5H10] validated for WB, IP, ICC/IF and tested in Mouse. Referenced in 2 publications and 1 independent review. Immunogen…
SCGF antibody [6D5] (C-type lectin domain family 11, member A) for IHC, WB. Anti-SCGF mAb (GTX52987) is tested in Human samples. 100% Ab-Assurance.
CLECSF6小鼠单克隆抗体[MM0237- 5P20](ab89188)可与人样本反应并经WB, Flow Cyt实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
|strong|Rabbit anti Human CD209 antibody|/strong| recognizes an epitope within the extracellular domain of human DC-SIGN. DC-SIGN was designated CD209 at the 7th leucocyte typing workshop. |br||br|Ra…
Входит в надсемейство белков лектины C-типа/лектино-подобный домен C-типа (CTL/CTLD). Белки этого надсемейства имеют похожую конформацию и обладают различными функциями, включая клеточную адгезию, межклеточную передачу сигнала, обмен гликопротеинов, участие в воспалении и иммунном ответе. CLL-1 является отрицательным регулятором гранулоцитарных и моноцитарных функций. ...
NK cells are the first line of defense against infected and transformed cells. Defective NK cell activity was shown to increase susceptibility for viral infections and reduce tumor immune-surveillance. With age, the incidence of infectious diseases and malignancy rises dramatically, suggesting that impaired NK cell function might contribute to disease in these individuals. We found an increased frequency of NK cells with high expression of the inhibitory killer cell lectin-like receptor G1 (KLRG1) in individuals |70 y. The role of KLRG1 in ageing is not known, and the mechanism of KLRG1-induced inhibition of NK cell function is not fully understood. We report that NK cells with high KLRG1 expression spontaneously activate the metabolic sensor AMP-activated protein kinase (AMPK) and that activation of AMPK negatively regulates NK cell function. Pre-existing AMPK activity is further amplified by ligation of KLRG1 in these cells, which leads to internalization of the receptor and allows interaction with
NK cells are the first line of defense against infected and transformed cells. Defective NK cell activity was shown to increase susceptibility for viral infections and reduce tumor immune-surveillance. With age, the incidence of infectious diseases and malignancy rises dramatically, suggesting that impaired NK cell function might contribute to disease in these individuals. We found an increased frequency of NK cells with high expression of the inhibitory killer cell lectin-like receptor G1 (KLRG1) in individuals |70 y. The role of KLRG1 in ageing is not known, and the mechanism of KLRG1-induced inhibition of NK cell function is not fully understood. We report that NK cells with high KLRG1 expression spontaneously activate the metabolic sensor AMP-activated protein kinase (AMPK) and that activation of AMPK negatively regulates NK cell function. Pre-existing AMPK activity is further amplified by ligation of KLRG1 in these cells, which leads to internalization of the receptor and allows interaction with
Looking for online definition of C-type lectin domain family 4, member J in the Medical Dictionary? C-type lectin domain family 4, member J explanation free. What is C-type lectin domain family 4, member J? Meaning of C-type lectin domain family 4, member J medical term. What does C-type lectin domain family 4, member J mean?
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KLRC3, human recombinant protein, Killer cell lectin-like receptor subfamily C, NKG2-E; NKG2E validated in (PBV10978r-100), Abgent
Patients with cancer have an increased risk of thromboembolism, which is the second leading cause of death in these patients. Several mechanisms of the prothrombotic state in these patients have been proposed. Among them are a platelet activation receptor, C-type lectin-like receptor 2 (CLEC-2), and its endogenous ligand podoplanin, which are the focus of this review. CLEC-2 is almost specifically expressed in platelets/megakaryocytes in humans. A membrane protein, podoplanin is expressed in certain types of cancer cells, including squamous cell carcinoma, brain tumor, and osteosarcoma, in addition to several normal tissues, including kidney podocytes and lymphatic endothelial cells but not vascular endothelial cells. In the bloodstream, podoplanin induces platelet activation by binding to CLEC-2 and facilitates hematogenous cancer metastasis and cancer-associated thrombosis. In an experimental lung metastasis model, the pharmacological depletion of CLEC-2 from platelets in mice resulted in a ...
The ability of a peptide vaccine to stimulate T cells in vivo might be improved by specifically targeting the peptide to dendritic cells (DC). The C-type lectin Macrophage Galactose-type lectin, MGL (CD301), has been shown to bind to N-acetyl-galactosamine (GalNAc) and small peptides bearing O-linked GalNAc. Synthetic GalNAc can be produced using relatively simple organic chemistry when compared with the complicated branched sugars that are recognised by other C-type lectins. MGL therefore represents a promising target for the design of synthetic peptide vaccines. We have identified that antigen-presenting cells in human skin express MGL and have confirmed that CD14+ dermal DCs might be targeted via MGL. The intracellular fate of MGL following internalisation was tracked by confocal microscopy. MGL traffics through early endosomes to late endosomes/lysosomes, and colocalises with MHC class I and class II. Synthetic glycopeptides were produced incorporating either native O-linked GalNAc or GalNAc ...