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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. Additionally we are shipping CD209 Molecule Proteins (13) and CD209 Molecule Kits (7) and many more products for this protein.
Showing 10 out of 281 products:
Human Polyclonal CD209 Primary Antibody for WB - ABIN871703
Engering, Geijtenbeek, van Vliet, Wijers, van Liempt, Demaurex, Lanzavecchia, Fransen, Figdor, Piguet, van Kooyk: The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for presentation to T cells. in Journal of immunology (Baltimore, Md. : 1950) 2002
Show all 3 references for ABIN871703
Human Monoclonal CD209 Primary Antibody for FACS - ABIN320225
Relloso, Puig-Kröger, Pello, Rodríguez-Fernández, de la Rosa, Longo, Navarro, Muñoz-Fernández, Sánchez-Mateos, Corbí: DC-SIGN (CD209) expression is IL-4 dependent and is negatively regulated by IFN, TGF-beta, and anti-inflammatory agents. in Journal of immunology (Baltimore, Md. : 1950) 2002
Show all 2 references for ABIN320225
Human Monoclonal CD209 Primary Antibody for FACS - ABIN181973
Melero, Gabari, Corbí, Relloso, Mazzolini, Schmitz, Rodriguez-Calvillo, Tirapu, Camafeita, Albar, Prieto: An anti-ICAM-2 (CD102) monoclonal antibody induces immune-mediated regressions of transplanted ICAM-2-negative colon carcinomas. in Cancer research 2002
Show all 2 references for ABIN181973
Human Monoclonal CD209 Primary Antibody for FACS, IF - ABIN1106050
Khoo, Chan, Chan, Lin: DC-SIGN and L-SIGN: the SIGNs for infection. in Journal of molecular medicine (Berlin, Germany) 2008
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.
The cloning and characterization of the cDNA and gene encoding porcine DC-SIGN (pDC (show PDC Antibodies)-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
The high-mannose N-linked glycan at N154 of Japanese encephalitis virus E glycoprotein was shown to be crucial for binding to DC-SIGN and subsequent internalization.
Preliminary study suggests that OAS (show SMOC1 Antibodies) gene cluster and CD209 gene polymorphisms influence the risk of developing clinical symptoms in Chikungunya virus-infected patients.
DC-SIGN can promote the maturation and activation of dendritic cells on recognition of hepatitis B virus, but wild type virus can escape recognition by DC-SIGN to a certain extent with the help of demannosylated modification.
Colorectal mucus can bind the C-type lectin (show MBL2 Antibodies) DC-SIGN and block HIV-1 trans-infection of both CCR5 (show CCR5 Antibodies) and CXCR4 (show CXCR4 Antibodies) using HIV-1 strains.
Engagement of sIg (show PICALM Antibodies) in FL cells or normal B cells by anti-Ig led to endocytosis in vitro as expected, but DC-SIGN, even when cross-linked, did not lead to significant endocytosis of sIg (show PICALM Antibodies)
M2 macrophages induced a DC-SIGN-dependent adhesion of highly mannosylated IgM(+) FL B cells and triggered BCR (show BCR Antibodies)-associated kinase activation.
DC-SIGN-induced ISGF3 (show STAT1 Antibodies) by fucose-based PAMPs has an essential role in driving IL-27 (show IL27 Antibodies) and subsequent TFH polarization, which might be harnessed for vaccination design
selective engagement of dendritic cell-SIGN resulting in intracellular persistence in myeloid dendritic cells; however TLR2 (show TLR2 Antibodies) activation can overcome autophagy evasion and pathogen persistence in dendritic cells
High-resolution crystal structures of the SIGN-R1 carbohydrate recognition domain show 2 binding sites allowing SIGNR1 (show CD209B Antibodies) to simultaneously bind both immune glycoproteins and microbial polysaccharide components.
Data suggest that serum amyloid P (SAP (show APCS Antibodies)) activates CD209 DC-SIGN to regulate the innate immune system differently from C-reactive protein (CRP (show CRP Antibodies)), and that DC-SIGN is a target for antifibrotics.
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.
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
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 (show PDCD1LG2 Antibodies)(+) 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 (show LECT2 Antibodies).
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 (show CRX Antibodies) of DC-SIGN and the extracellular matrix and/or cis (show CISH Antibodies) interactions with transmembrane scaffolding protein(s) play an essential role in organizing these microdomains
analysis of activated apoptotic cells induce dendritic cell maturation via engagement of Toll-like receptor 4 (TLR4 (show TLR4 Antibodies)), dendritic cell-specific intercellular adhesion molecule 3 (ICAM-3 (show ICAM3 Antibodies))-grabbing nonintegrin (DC-SIGN), and beta2 integrins
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.
, CD209-like protein
, C-type lectin domain family 4, member M
, DC-SIGN protein
, C-type lectin domain family 4 member L
, C-type lectin domain family 4, member L
, HIV gpl20-binding protein
, dendritic cell-specific ICAM-3-grabbing non-integrin 1
, dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin
, dendritic cell-specific ICAM-3 grabbing non-integrin
, 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