The paired immunoglobulin-like type 2 receptor beta (PILRB) is a cell surface receptor belonging to the immunoglobulin superfamily, primarily expressed on immune cells such as macrophages, neutrophils, and dendritic cells. It interacts with ligands like PILRA (its paired receptor) and certain glycosylated proteins, playing roles in immune regulation, cell signaling, and inflammatory responses. PILRB is implicated in modulating both activating and inhibitory pathways, with its cytoplasmic tail containing immunoreceptor tyrosine-based inhibitory motifs (ITIMs) that recruit phosphatases to dampen cellular activation.
PILRB antibodies are tools developed to study receptor-ligand interactions, downstream signaling, and its involvement in diseases. Research highlights its association with neuroinflammatory conditions (e.g., Alzheimer’s disease) and autoimmune disorders, where dysregulated PILRB activity may contribute to pathological inflammation or immune evasion. Antibodies targeting PILRB are utilized in functional assays (e.g., blocking ligand binding), flow cytometry, and immunohistochemistry to explore its expression patterns and therapeutic potential. Recent studies also investigate PILRB's role in cancer immunity and viral infections, as some pathogens exploit PILRB-related pathways to evade immune detection. Challenges include understanding receptor redundancy and species-specific differences, as murine PILRB homologs differ functionally from human counterparts. These antibodies hold promise for dissecting immune modulation mechanisms and developing targeted therapies.