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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P12989(SIGLECL1 Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

SIGLECL1 (Sialic acid-binding immunoglobulin-like lectin L1) is a member of the Siglec family, a group of cell surface receptors characterized by immunoglobulin-like domains that bind sialic acid-containing glycans. It shares structural homology with CD33-related Siglecs, featuring an N-terminal V-set Ig domain for ligand recognition, followed by variable C2-type Ig domains, a transmembrane region, and cytoplasmic tyrosine-based signaling motifs. Although its exact biological role remains less defined compared to well-studied Siglecs (e.g., CD33. Siglec-7), SIGLECL1 is implicated in immune regulation, potentially modulating cell-cell interactions and inflammatory responses in innate immunity.

SIGLECL1 antibodies are research tools designed to detect, quantify, or inhibit this protein in experimental settings. They enable studies on its expression patterns, which are reported in subsets of immune cells (e.g., monocytes, dendritic cells) and certain malignancies, suggesting a role in immune evasion or tumor microenvironment signaling. These antibodies are pivotal in techniques like flow cytometry, immunohistochemistry, and Western blotting to explore SIGLECL1's involvement in diseases, including cancer and autoimmune disorders. Recent interest has emerged in its potential as an immune checkpoint molecule, with therapeutic antibodies under preclinical investigation for targeting Siglec-mediated immunosuppression. However, challenges persist in clarifying its ligands, signaling pathways, and functional redundancy within the Siglec family, necessitating further validation of antibody specificity and functional assays.