Transthyretin (TTR) antibodies are primarily studied in the context of TTR amyloidosis (ATTR), a disorder caused by the misfolding and aggregation of TTR protein into amyloid fibrils, leading to organ dysfunction. TTR, a tetrameric protein produced in the liver and choroid plexus, normally transports thyroxine and retinol. Genetic mutations or aging can destabilize TTR, promoting dissociation into monomers that misfold and aggregate. Antibodies targeting TTR have emerged as therapeutic tools to inhibit amyloid formation or clear existing deposits. Some monoclonal antibodies bind to misfolded TTR epitopes, preventing fibril formation or promoting phagocytic clearance. Research also explores autoantibodies against TTR in autoimmune diseases, though their clinical significance remains unclear. Additionally, TTR antibody-based assays aid in diagnosing ATTR amyloidosis by detecting amyloid deposits in tissues. Recent therapies, like tafamidis (a TTR stabilizer) and siRNA/antisense oligonucleotides, indirectly relate to antibody strategies by reducing pathogenic TTR levels. Immunotherapy using engineered antibodies represents a promising avenue to directly target amyloidogenic TTR species, offering potential for disease modification in ATTR.