Cayman DC-SIGN1/CD209 Extracellular Domain (human, recombinant)

Dendritic cell-specific ICAM-3-grabbing non-integrin 1 (DC-SIGN1), also known as CD209, is a type II transmembrane glycoprotein and member of the C-type lectin receptor superfamily.^1,2 It is composed of an N-terminal cytoplasmic domain, a transmembrane domain, a neck region that contains seven repeats of 23 amino acids and is involved in oligomerization, and a carbohydrate recognition domain. However, DC-SIGN1 undergoes extensive alternative splicing that results in at least 12 membrane-bound or soluble isoforms.^1,3 It is expressed in dendritic cells and macrophages, dermal, mucosal, intestine, and lung tissues, as well as blood and lymph nodes.^1,2 DC-SIGN1 is involved in cell-cell adhesion and migration via interactions with intracellular cell adhesion molecule-2 (ICAM-2) and ICAM-3, recognition of viral and bacterial pathogens, and the immune response.^1,2,4 It binds to HIV-1 gp120 and the receptor-binding domain of spike glycoprotein, also known as surface glycoprotein, of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).^5,6 Dendritic cell expression of human CD209 increases survival in a mouse model of M. tuberculosis infection.⁴ SNPs in CD209 are associated with increased disease severity in patients with dengue viral infection.⁷ Cayman’s DC-SIGN1/CD209 Extracellular Domain (human, recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of DC-SIGN1 (amino acids 62-404) fused to human IgG1 Fc at its N-terminus, consists of 580 amino acids and has a calculated molecular weight of 65.8 kDa. As a result of glycosylation, the monomer migrates at approximately 75 kDa by SDS-PAGE under reducing conditions.

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