CD209a Monoclonal Antibody (LWC06), APC, eBioscience™, Invitrogen™

Description

• Description: The LWC06 antibody was generated by immunization with the recombit extracellular region of mouse CIRE/DC-SIGN (CD209)
• CIRE/DC-SIGN was identified by its expression on CD8 alpha- dendritic cells and plasmacytoid predendritic cells, and is the closest homologue of human DC-SIGN
• Human DC-SIGN was originally identified in human placenta for its ability to bind the HIV envelope protein gp120 in a CD4-independent manner
• CIRE/DC-SIGN is a 33 kDa type II transmembrane C-type lectin protein
• It contains a C-terminal, extracellular, Carbohydrate Recognition Domain (CRD) that is predicted to bind mannose and other carbohydrates in a calcium dependent manner
• It has been postulated that CIRE/DC-SIGN may play a role in T-dendritic cell interactions through binding with members of the ICAM family
• CIRE/DC-SIGN is differentially expressed by sub-populations of dendritic cells and preliminary data suggest that its expression varies depending on the activation state of the host
• CIRE/DC-SIGN is down-regulated in spleen-derived dendritic cell cultures supplemented with GM-CSF
• While human DC-SIGN is predomitly expressed in dendritic cells, CIRE/DC-SIGN mRNA has also been detected in B cells
• The LWC06 monoclonal antibody does not cross-react with the closely related SIGNR1, SIGNR2, SIGNR3 or SIGNR4
• CD209 protein is sensitive to collagenase treatment
• Applications Reported: This LWC06 antibody has been reported for use in flow cytometric analysis
• 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.