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CLEC10A encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Zusätzlich bieten wir Ihnen CLEC10A Antikörper (143) und CLEC10A Proteine (23) und viele weitere Produktgruppen zu diesem Protein an.
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this paper shows that key gene of intermediate proinflammatory monocytes, such as CLEC10A, is expressed three- to fourfold more in juvenile idiopathic arthritis-enthesitis-related arthritis
BRAF (zeige BRAF ELISA Kits)(V600E) mutation induces MGL ligand expression, thereby providing a direct link between oncogenic transformation and aberrant expression of immunosuppressive glycans in colorectal neoplasms.
These results indicate a role of MGL as an immunomodulator within the tumour microenvironment interfering with Treg functions, suggesting its possible use in the design of anticancer vaccines.
expression of GalNAc moieties mirrors the T cell activation status, and thus only highly stimulated T cells are prone to the suppressive action of MGL.
MGL triggering synergized with TLR2-induced pathways, leading to elevated IL-10 (zeige IL10 ELISA Kits) mRNA levels & enhanced TNF-alpha (zeige TNF ELISA Kits) mRNA stability. It promoted phosphorylation of the ERK (zeige EPHB2 ELISA Kits) & CREB (zeige CREB1 ELISA Kits), fine-tuning the DC maturation phenotype.
Described is the use of recombinant CLEC10A (CD301), a human glycoreceptor of the C-type lectin (zeige MBL2 ELISA Kits) family, for the detection of ligands in sections from formalin-fixed, paraffin-embedded normal and cancerous mammary tissues.
MGL engagement improved DC performance as antigen-presenting cells, promoting the upregulation of maturation markers, a decrease in phagocytosis, an enhancement of motility, and most importantly an increase in antigen-specific CD8 (zeige CD8A ELISA Kits)(+) T-cell activation.
Macrophage Galactose-Type Lectin-1 Deficiency Is Associated with Increased Neutrophilia and Hyperinflammation in Gram-Negative Pneumonia
Mgl1-deficient mice displayed accelerated colonic propulsion and were hypersensitive to mu receptor-mediated inhibition of colonic motility.
MGL1 is involved in T. crassiceps recognition and subsequent innate immune activation and resistance.
The MGL1 functions as an attachment and entry receptor for influenza A virus.
Syk was involved in the CLR-mediated activation of mast cells by BP
Hoxc8 downregulates Mgl1 tumor suppressor gene expression and reduces its concomitant function on cell adhesion.
The authors conclude that lectin-mediated interactions of influenza virus with the MMR (zeige MRC1 ELISA Kits) or the MGL are required for the endocytic uptake of the virus into macrophages.
mMGL1 preferentially binds Lewis X (zeige FUT4 ELISA Kits)-conjugated soluble polyacrylamides
Generation of mice deficient for macrophage galactose- and N-acetylgalactosamine-specific lectin: limited role in lymphoid and erythroid homeostasis and evidence for multiple lectins.
sialoadhesin (zeige SIGLEC1 ELISA Kits) acts as an endogenous counter-receptor for MGL1
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 function as a cell surface antigen. Two transcript variants encoding distinct isoforms have been identified for this gene.
C-type lectin domain family 10, member A
, C-type lectin, superfamily member 14
, C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 13 (macrophage-derived)
, C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 14 (macrophage-derived)
, C-type lectin domain family 10 member A
, macrophage lectin 2 (calcium dependent)
, macrophage asialoglycoprotein-binding protein 1
, macrophage galactose N-acetyl-galactosamine specific lectin 1
, Gal/GalNAc-specific lectin
, macrophage galactose/N-acetylgalactosamine-specific lectin
, monoglyceride lipase