Anti-Human SIGLEC1 Antibody Pair

Product Description: Sialic acid binding Ig like lectin 1 (SIGLEC1), also known as sialoadhesin and CD169, is a 175-185 kDa glycoprotein belonging to the immunoglobulin superfamily. It is a type I transmembrane protein expressed primarily by a subpopulation of macrophages and plays a crucial role in mediating cell-cell interactions through sialic acid-dependent binding to glycoconjugate ligands on cell surfaces. The protein contains an N-terminal Ig-like V-set domain and 16 Ig-like C2-set domains, which preferentially bind to alpha-2,3-linked sialic acid residues. SIGLEC1 is involved in various biological processes, including phagocytosis of sialylated bacteria and viruses, and it enhances macrophage-to-T-cell transmission of viruses such as HIV-1 and SARS-CoV-2. Diseases associated with SIGLEC1 include rheumatoid arthritis and heart block, and it has been implicated in systemic lupus erythematosus and idiopathic inflammatory myopathies. Protein Function: Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a crucial role in limiting bacterial dissemination by engaging sialylated bacteria to promote effective phagocytosis and antigen presentation for the adaptive immune response (PubMed:12940982, PubMed:33489013). Mediates the uptake of various enveloped viruses via sialic acid recognition and subsequently induces the formation of intracellular compartments filled with virions (VCCs) (PubMed:28129379). In turn, enhances macrophage-to-T-cell transmission of several viruses including HIV-1 or SARS-CoV-2 (PubMed:28129379, PubMed:34782760). Acts as an endocytic receptor mediating clathrin dependent endocytosis. Preferentially binds to alpha-2,3-linked sialic acid (PubMed:12940982). Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis. Plays a role in the inhibition of antiviral innate immune by promoting TBK1 degradation via TYROBP and TRIM27-mediated ubiquitination (PubMed:26358190) , (Microbial infection) Facilitates viral cytoplasmic entry into activated dendritic cells via recognition of sialylated gangliosides pesent on viral membrane [The Uniprot Consortium]