Mouse Monoclonal TTR Antibody

Transthyretin (TTR) antibodies are primarily studied in the context of TTR-related amyloidosis (ATTR), a condition caused by misfolded TTR protein aggregates. TTR, a tetrameric transport protein synthesized by the liver, normally carries thyroxine and retinol-binding protein. In ATTR, destabilized TTR monomers misfold, forming amyloid fibrils that accumulate in tissues, leading to organ dysfunction. Antibodies targeting TTR play dual roles: diagnostic tools and therapeutic agents. Diagnostically, anti-TTR antibodies are used in immunohistochemistry or immunoassays (e.g., ELISA) to detect TTR deposits in biopsies or quantify serum TTR levels, aiding in disease confirmation and monitoring. Therapeutically, monoclonal antibodies (e.g., PRX004. NI301A) are designed to disrupt amyloid fibrils or stabilize TTR tetramers, slowing disease progression. Research also explores antibodies' ability to enhance clearance of toxic TTR aggregates via immune-mediated pathways. Challenges include ensuring antibody specificity to pathogenic forms without affecting functional TTR and overcoming physiological barriers like the blood-brain barrier in neural amyloidosis. Autoantibodies against TTR have been reported in some autoimmune conditions, though their clinical significance remains unclear. Current studies focus on optimizing antibody engineering for improved efficacy and reduced immunogenicity, with several candidates in preclinical or early clinical trials. These advancements highlight the growing importance of TTR antibodies in both understanding ATTR pathophysiology and developing targeted therapies.