Description: DC-SIGN Monoclonal Antibody: Dendritic cells (DCs) that control immune responses were recently found to capture and transport HIV from the mucosal area to remote lymph nodes, where DCs hand over HIV to CD4+ T lymphocytes. DCs also amplify the amount of virus and extend the duration of viral infectivity. Multiple strains of HIV-1, HIV-2 and SIV bind to DCs via DC-SIGN. ICAM-3 is the natural ligand for DC-SIGN. A DC-SIGN homologue (termed DC-SIGNR, L-SIGN, and DC-SIGN2) was identified recently. DC-SIGN forms a novel gene family with DC-SIGNR and many alternatively spliced isoforms of DC-SIGN and DC-SIGNR are known to exisit. The expression of DC-SIGN was found in mucosal tissues including placenta, small intestine, and rectum.

Description: DC-SIGN is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN / CD209 is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN / CD209 is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN / CD209 is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN/CD209 is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN/CD209 is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: DC-SIGN/CD209 is a transmembrane receptor that is expressed on the surface of dendritic cells and macrophages. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses. 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.

Description: (CT) DC-SIGN peptide

Description: Mouse polyclonal to DC-SIGN