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NSJ Bioreagents

SKU:V9406-20UG

CD209 Antibody / DC-SIGN, 20 ug

CD209 Antibody / DC-SIGN, 20 ug

Regular price $259.00 USD
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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.

Specifications

Catalog No V9406-20UG
Family Primary antibody
Qty 20 ug
Formulation 0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide
Format Purified
Clone C209/6774
Host Animal Mouse
Clonality Monoclonal (mouse origin)
Isotype Mouse IgG1, kappa
Species Reactivity Human
Application FACS
Application Details Flow cytometry: 1-2ug/million cells
Application Note Optimal dilution of the CD209 antibody should be determined by the researcher.
Localization Cell surface and secreted
Immunogen A recombinant human DC-SIGN/CD209 protein fragment was used as the immunogen for the CD209 antibody.
Purity Protein A/G affinity
Storage Aliquot the CD209 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Limitation This CD209 antibody is available for research use only.
Uniprot # Q9NNX6
Status Available
PDF Link https://www.nsjbio.com/tds-pdf/cd209-antibody-dc-sign-c2096774-v9406
Title CD209 Antibody / DC-SIGN
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.
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