Siglec-1/CD169 (E1D7G) Rabbit mAb recognizes endogenous levels of total Siglec-1/CD169 protein. This antibody does not cross-react with human Siglec-1/CD169 protein. Non-specific staining was observed in mouse pancreas and testis by immunohistochemistry.


Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro1229 of mouse Siglec-1/CD169 protein.

Sialic acid-binding Ig-like lectin 1 (Siglec-1/CD169) is a type-I transmembrane glycoprotein and a member of the siglec family of sialic acid-binding proteins. Structurally, Siglec-1 contains a heavily glycosylated extracellular domain and a short intracellular domain with no canonical signaling motifs (1). Expression of Siglec-1 is largely restricted to tissue-resident macrophages found in the bone marrow, liver, spleen, and lymph nodes. Research studies have shown that Siglec-1 is an adhesion molecule and binds to sialylated glycoconjugates to facilitate cell-cell and cell-matrix interactions (2-4). Siglec-1 has also been shown to facilitate the host innate immune response by binding to sialylated epitopes on the surface of viral and bacterial pathogens prior to initiating their phagocytosis (5,6). In the context of cancer, Siglec-1 has been shown to serve as a marker for subsets of proinflammatory macrophages in the tumor microenvironment that aid in the anti-tumor response by phagocytosing tumor cells and recruiting cytotoxic lymphocytes (7).