CD209 (DC-SIGN) Monoclonal Antibody (eB-h209), eBioscience™, Invitrogen™

Description

• Description: The eB-h209 monoclonal antibody reacts with human CD209, also known as DC-SIGN, a 44 kDa type II transmembrane protein
• DC-SIGN contains a C-type lectin binding domain and binds ICAM-3, ICAM-2, and HIV virus
• Human dendritic cells preferentially express DC-SIGN
• It has been postulated that DC-SIGN serves as a receptor for capture, trafficking, and transmission of HIV to T cells and supports primary immune response
• eB-h209 was developed against a C-terminal peptide of human DC-SIGN
• Applications Reported: The eB-h209 antibody has been reported for use in flow cytometric analysis, and immunoprecipitation
• Applications Tested: The eB-h209 antibody has been tested by flow cytometric analysis of cultured human dendritic cells and peripheral blood cells
• This can be used at less than or equal to 1 μg per test
• A test is defined as the amount (μg) of antibody that will stain a cell sample in a final volume of 100 μL
• Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test
• It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest
• Purity: Greater than 90%, as determined by SDS-PAGE
• Aggregation: Less than 10%, as determined by HPLC
• Filtration: 0.2 μm post-manufacturing filtered
• 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.