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Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. Paired immunoglobulin-like type 2 receptor alpha (PILRα) and PILRβ are paired receptors bearing highly similar extracellular ligand-binding domains but divergent intracellular signaling domains. PILRα is the immune inhibitory receptor possessing an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic domain enabling it to deliver inhibitory signals. Binding of PILRα to its ligand CD99 is involved in immune regulation. PILRα can also recognize other ligands, PILR-associating neural protein (PANP), and HSV-1 glycoprotein B (HSV-1 gB). PILRα has a calculated molecular weight of 34 kDa. It has been reported that PILRα migrates at 44-50 kDa due to glycosylation (PMID: 10903717; 10660620). The other band of about 61 kDa detected by this antibody may present a heavily glycosylated form of PILRα.