Species predicted to react based on 100% sequence homology:Monkey
Specificity / Sensitivity
DC-SIGN Antibody recognizes endogenous levels of total DC-SIGN protein. This antibody also detects DC-SIGNR.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val134 of human DC-SIGN protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
DC-SIGN (CD209/CLEC4L) is a C-type lectin receptor expressed by dendritic cells (DCs) (1,2). The DC-SIGN transcript can undergo several splicing events to generate at least thirteen different transmembrane and soluble isoforms (3). DC-SIGN responds to a broad range of pathogens due to its ability to recognize both mannose and fructose carbohydrates, and is well-studied for its role in HIV infection. Recognition of the HIV envelope glycoprotein gp120 by DC-SIGN leads to internalization of HIV by DCs and facilitates transmission of the virus to CD4+ T cells (2,4). DC-SIGN also mediates adhesion to T cells through interaction with ICAM-3, as well as transmigration across the endothelium by binding to ICAM-2 (1,5). DC-SIGN can also modulate TLR signaling by activating the kinase Raf-1 (6,7). DC-SIGNR (L-SIGN/CLEC4M) is a closely related molecule that is 77% homologous to DC-SIGN and likely arose through a gene duplication event (8). Like DC-SIGN, DC-SIGNR binds mannose carbohydrates on the surface of pathogens (8,9). However, the expression patterns of the two receptors differ, as DC-SIGNR expression is restricted to endothelial cells of the liver, lymph node, and placenta (10). In mice, there is a set of related molecules, SIGNR1-SIGNR8 (11). Based on sequence analysis, there is no clear ortholog to human DC-SIGN, however SIGNR3 is the most functionally similar due to its ability to recognize both mannose and fructose structures (11).