The immunoglobulin superfamily member 8 (IGSF8), also known as PGRL or KU-ID, is a transmembrane protein belonging to the immunoglobulin superfamily. It contains two extracellular immunoglobulin-like domains and is implicated in cell-cell adhesion, immune regulation, and intracellular signaling. IGSF8 is broadly expressed in immune cells, endothelial cells, and certain epithelial tissues, where it interacts with proteins like junctional adhesion molecules (JAMs) and integrins to modulate immune responses, cell polarity, and barrier function.
Antibodies targeting IGSF8 are primarily used as research tools to investigate its biological roles. They enable the detection, localization, and functional analysis of IGSF8 in experimental models, including cancer, inflammatory diseases, and neurological disorders. Studies suggest IGSF8 may influence tumor progression by regulating immune evasion or metastatic pathways, while its involvement in endothelial cell adhesion highlights potential roles in vascular permeability and leukocyte trafficking.
Commercially available IGSF8 antibodies are typically monoclonal or polyclonal, generated in hosts like rabbits or mice, and validated for applications such as Western blotting, immunohistochemistry, and flow cytometry. Challenges include ensuring specificity due to shared epitopes within the immunoglobulin superfamily. Recent research explores IGSF8's therapeutic potential, with antibodies being tested for diagnostic or immune-modulatory applications. However, its precise mechanistic contributions remain under investigation, necessitating further studies to clarify its pathophysiological relevance.