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CD209 encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages. Zusätzlich bieten wir Ihnen CD209 Molecule Antikörper (496) und CD209 Molecule Proteine (18) und viele weitere Produktgruppen zu diesem Protein an.
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These results show that DC-SIGN and TLR-4 (zeige TLR4 ELISA Kits) interactions regulate inflammatory responses in renal tubular epithelial cells and participate in AKI pathogenesis.
1,25(OH)2D3 suppressed the DCSIGN expression in Mycobacterium tuberculosis infected onocytes/macrophages.
Studied the association of CD209 promoter haplotypes with risk of HIV-1 infection in a cohort of Spanish male intravenous drug users (IDU) infected with hepatitis C virus (HCV).
Upon gp120 (zeige ITIH4 ELISA Kits) binding to DC-SIGN, cellular NF-kappaB (zeige NFKB1 ELISA Kits) signaling was triggered, leading to the induction of matrix metalloproteinases, which subsequently degraded tight junction proteins and disrupted the blood-retinal barrier integrity.
This study showed that N-glycans on the Gc and Gn surface glycoproteins redundantly support Rift Valley Fever Virus infection via DC-SIGN.
Ligand-driven triggering of TLR-3 (zeige TLR3 ELISA Kits), -4, NOD2 (zeige NOD2 ELISA Kits), and DC-SIGN, despite reducing viral replication, markedly increased the capacity of infected dendritic cells to stimulate HIV-specific cytotoxic T-cells.
CD209 polymorphisms could play a role in the susceptibility to Hepatitis C infection as well as interferon (zeige IFNA ELISA Kits) treatment response
The activation of B cells enhances DC-SIGN expression and promotes susceptibility of B cells to the avian H5N1 infection.
Binding of common allergens by DC-SIGN on DCs may initiate allergen sensitization of atopic dermatitis or provoke the relapse of atopic dermatitis
These results suggest that DC-SIGN may be an alternative receptor for influenza A(H1N1)pdm09 virus.
The development and use of CD209 to characterize the phenotype of CD209 expressing cells in bovine blood using flow cytometry is reported.
a DC-SIGN-like molecule expressed specifically by bovine DC. This molecule may play an important role in the infection of bovine (DC) cells with M. bovis.
DC-SIGN+ cells showed a clear differential distribution in the decidua in the first 2 weeks of pregnancy, being found only adjacent to the implantation site
DC-SIGN expression in mesenteric lymph nodes is significantly downregulated in simian immunodeficiency virus-infected pig-tailed macaques.
The cloning and characterization of the cDNA and gene encoding porcine DC-SIGN (pDC (zeige PDC ELISA Kits)-SIGN)is reported. The results will help better understand the biological role(s) of DC-SIGN family in innate immunity during the evolutionary process.
identification and functional characterization of DC-SIGN/CD209 molecule in zebrafish
M. scrofulaceum induces a semimature DC phenotype that is characterized by PD-L2 (zeige PDCD1LG2 ELISA Kits) over-expression and elevated synthesis of IL-10 (zeige IL10 ELISA Kits), most likely through TLR4 (zeige TLR4 ELISA Kits) and Raf-1 (zeige RAF1 ELISA Kits) signaling pathway-dependent DC-SIGN stimulation.
results suggested that podocytes in lupus nephritis can exert dendritic cell-like function through their expression of DC-SIGN, which may be involved in immune and inflammatory responses of renal tissues
High-resolution crystal structures of the SIGN-R1 carbohydrate recognition domain show 2 binding sites allowing SIGNR1 to simultaneously bind both immune glycoproteins and microbial polysaccharide components.
Data suggest that serum amyloid P (SAP (zeige APCS ELISA Kits)) activates CD209 DC-SIGN to regulate the innate immune system differently from C-reactive protein (CRP (zeige CRP ELISA Kits)), and that DC-SIGN is a target for antifibrotics.
Intestinal enterocytes regulate tissue-associated immune compartments under the control of DC-SIGN in inflammatory bowel disease.
In vivo T cell activation induces the formation of CD209(+) PDL-2 (zeige PDCD1LG2 ELISA Kits)(+) dendritic cells.
CD209a expression on dendritic cells is critical for the development of pathogenic Th17 cell responses in murine schistosomiasis.
CD209a is activated in macrophages by LECT2 (zeige LECT2 ELISA Kits).
The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells
interactions between the CRD (zeige CRX ELISA Kits) of DC-SIGN and the extracellular matrix and/or cis (zeige CISH ELISA Kits) interactions with transmembrane scaffolding protein(s) play an essential role in organizing these microdomains
This gene encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages. The encoded protein is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses with a large impact on public health. The protein is organized into three distinct domains: an N-terminal transmembrane domain, a tandem-repeat neck domain and C-type lectin carbohydrate recognition domain. The extracellular region consisting of the C-type lectin and neck domains has a dual function as a pathogen recognition receptor and a cell adhesion receptor by binding carbohydrate ligands on the surface of microbes and endogenous cells. The neck region is important for homo-oligomerization which allows the receptor to bind multivalent ligands with high avidity. Variations in the number of 23 amino acid repeats in the neck domain of this protein are rare but have a significant impact on ligand binding ability. This gene is closely related in terms of both sequence and function to a neighboring gene (GeneID 10332\; often referred to as L-SIGN). DC-SIGN and L-SIGN differ in their ligand-binding properties and distribution. Alternative splicing results in multiple variants.
C-type lectin domain family 4 member L
, C-type lectin domain family 4, member L
, CD209 antigen
, HIV gpl20-binding protein
, dendritic cell-specific ICAM-3-grabbing non-integrin 1
, dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin
, CD209-like protein
, dendritic cell-specific ICAM-3 grabbing non-integrin
, C-type lectin domain family 4, member M
, DC-SIGN protein
, putative mannose-binding C-type lectin
, CD209 antigen-like protein A
, dendritic cell-specific ICAM-3-grabbing non-integrin
, CD209 antigen-like protein C
, CD209c antigen
, Dendritic cell-specific ICAM-3-grabbing non-integrin 1
, dendritic cell-specific ICAM-3 grabbing nonintegrin