LRIG1 (Leucine-rich repeats and immunoglobulin-like domains 1) is a transmembrane protein belonging to the LRIG family, which includes LRIG2 and LRIG3. It is characterized by leucine-rich repeats (LRRs) and immunoglobulin-like domains in its extracellular region. LRIG1 functions as a tumor suppressor by negatively regulating receptor tyrosine kinases (RTKs), such as EGFR family members, through promoting their ubiquitination and degradation. This regulatory role impacts cell proliferation, differentiation, and survival, linking LRIG1 to cancer biology and tissue homeostasis. Reduced LRIG1 expression is observed in various cancers, including glioblastoma, breast cancer, and squamous cell carcinoma, and its loss often correlates with poor prognosis.
Antibodies targeting LRIG1 are essential tools for studying its expression, localization, and interactions. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and flow cytometry. These antibodies help elucidate LRIG1's tissue-specific distribution, its dynamic regulation during pathological processes, and its interplay with signaling pathways. Some antibodies specifically recognize extracellular epitopes, enabling the study of LRIG1's ligand-binding properties, while others target intracellular domains for functional assays.
Researchers also utilize LRIG1 antibodies to explore its role in stem cell biology, as LRIG1 marks stem cell populations in tissues like the epidermis and intestine. Validation of antibody specificity, species cross-reactivity (human, mouse, rat), and compatibility with experimental models (e.g., formalin-fixed vs. frozen samples) remains critical for reliable data. Commercial LRIG1 antibodies are available from multiple suppliers, often with distinct validation profiles.