TPR antibodies target proteins containing tetratricopeptide repeat (TPR) domains, which are structural motifs involved in mediating protein-protein interactions. These domains, typically composed of 34 amino acids arranged in repeating α-helical units, enable TPR-containing proteins to act as scaffolds in multiprotein complexes. TPR proteins are widely distributed across eukaryotes and play critical roles in diverse cellular processes, including cell cycle regulation, transcriptional control, mitochondrial protein import, and nuclear transport. For example, components of the nuclear pore complex (e.g., NUP98. NUP214) and the anaphase-promoting complex/cyclosome (APC/C) contain TPR domains.
Antibodies against TPR proteins are valuable tools in biomedical research. They are used to study subcellular localization, protein interactions, and functional dynamics in normal and pathological states. Dysregulation of TPR-containing proteins is linked to diseases such as cancer, neurodegenerative disorders, and autoimmune conditions. For instance, chromosomal translocations involving TPR-containing nucleoporins (e.g., NUP214-ABL1 fusion) are associated with leukemia. TPR antibodies also aid in diagnosing autoimmune diseases, as anti-TPR autoantibodies are detected in conditions like primary biliary cholangitis.
Research on TPR antibodies continues to expand, driven by their utility in elucidating molecular mechanisms and therapeutic targeting of TPR-associated pathways.