Tripeptidylpeptidase II (TPP2) is a large, multifunctional serine protease belonging to the subtilisin-like protease family. It is widely expressed in eukaryotic cells and primarily localized in the cytoplasm, though it can also associate with membranes or extracellular compartments under specific conditions. TPP2 functions as an exopeptidase, sequentially removing tripeptides from the N-terminus of polypeptides, complementing the proteasome in protein degradation. It plays roles in regulating peptide turnover, antigen processing, cell cycle progression, and apoptosis.
Antibodies targeting TPP2 are essential tools for studying its expression, localization, and function in physiological and pathological contexts. These antibodies are typically developed in rabbits or mice using immunogenic peptide sequences or recombinant protein fragments. They enable detection of TPP2 via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Research applications include investigating TPP2's involvement in immune responses, neurodegenerative diseases (e.g., Alzheimer’s), cancer progression (via apoptosis evasion), and autoimmune disorders. For example, TPP2 knockdown or inhibition studies using specific antibodies have revealed its role in modulating NF-κB signaling and cellular stress responses.
Commercial TPP2 antibodies vary in clonality (monoclonal/polyoclonal) and epitope specificity, requiring validation for cross-reactivity and target affinity. Dysregulation of TPP2 has been linked to chemotherapy resistance and viral infection mechanisms, highlighting its therapeutic relevance. Ongoing studies leverage these antibodies to explore TPP2 as a biomarker or therapeutic target in precision medicine.