Rabbit Polyclonal LBR Antibody

The lamin B receptor (LBR) is a nuclear membrane protein encoded by the *LBR* gene, primarily involved in chromatin binding and maintaining nuclear envelope structure. LBR antibodies are autoantibodies targeting this receptor, often studied in the context of autoimmune and genetic disorders. Initially identified in patients with rare conditions like Greenberg dysplasia and Pelger-Huët anomaly, LBR dysfunction is linked to disrupted neutrophil nuclear segmentation (pseudo-Pelger-Huët anomaly) and skeletal defects. In autoimmune diseases, anti-LBR antibodies are less common but have been detected in systemic lupus erythematosus (SLE) and anti-phospholipid syndrome (APS), though their clinical significance remains unclear compared to hallmark autoantibodies (e.g., anti-dsDNA). LBR's role in cholesterol biosynthesis and chromatin organization suggests potential connections between autoimmunity and cellular metabolism. Detection methods include indirect immunofluorescence, which may show nuclear rim staining on HEp-2 cells, and immunoblotting using recombinant LBR proteins. Research continues to explore whether these antibodies contribute to pathogenesis or serve as secondary markers of nuclear damage. Their rarity limits routine clinical use, but they remain valuable in studying nuclear envelope-related pathologies and autoimmune mechanisms.