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 immunoprecipitation, and immunoblotting (WB).Applications Tested: This LWC06 antibody has been tested by immunoblotting and immunoprecipitation of CIRE in CIRE-transfected CHO cells. The reactivity of this antibody has been confirmed by immunoprecipitation of CIRE with LWC06 followed by immunoblotting with another CIRE-specific monoclonal antibody, 5H10 (cat. 14-2091) and, immunoprecipitation of CIRE with 5H10 followed by immunoblotting with LWC06. 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.
|Immunoprecipitation, Western Blot|
|PBS with 0.09% sodium azide; pH 7.2|
For Research Use Only.
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