Ribosomal Protein SA (RPSA), also known as LamR1 (Laminin Receptor 1) or 37/67 kDa laminin receptor, is a multifunctional protein encoded by the RPSA gene. Initially identified as a ribosomal component involved in protein biosynthesis, RPSA was later discovered to function as a cell-surface receptor for laminin, a key extracellular matrix protein. This dual role links RPSA to diverse cellular processes, including ribosome assembly, cell adhesion, migration, and signaling. Structurally, RPSA comprises an N-terminal ribosomal-binding domain and a C-terminal laminin-binding domain, enabling its participation in both intracellular translational machinery and extracellular matrix interactions.
RPSA antibodies are essential tools for studying its expression, localization, and function in physiological and pathological contexts. In cancer research, RPSA overexpression is associated with tumor progression and metastasis, as laminin-mediated interactions promote invasive behavior. Antibodies targeting RPSA help detect its expression in tumor tissues or evaluate its role in cancer cell migration assays. In neurodegenerative diseases, RPSA is implicated in prion protein and amyloid-β trafficking, making these antibodies valuable for investigating Alzheimer’s or prion disease mechanisms. Additionally, RPSA serves as a receptor for pathogens like dengue virus and *Staphylococcus aureus*, highlighting its relevance in infectious disease studies. Commercial RPSA antibodies include monoclonal and polyclonal variants, often validated for applications such as Western blotting, immunofluorescence, and flow cytometry. Ongoing research continues to explore RPSA’s therapeutic potential as a biomarker or drug target.