TIPRL (TOR Signaling Pathway Regulator-like Protein) is a conserved eukaryotic protein implicated in regulating the TOR (Target of Rapamycin) signaling pathway, a central hub for cell growth, proliferation, and autophagy. First identified in yeast, TIPRL homologs in mammals interact with protein phosphatase 2A (PP2A), a key phosphatase involved in diverse cellular processes. TIPRL acts as a PP2A inhibitory regulator by binding to its catalytic subunit, modulating phosphatase activity and influencing downstream targets of mTORC1 (mechanistic Target of Rapamycin Complex 1). This interaction links TIPRL to nutrient sensing, stress responses, and cancer progression. Studies show TIPRL overexpression in several cancers, including hepatocellular carcinoma, lung cancer, and cervical cancer, where it promotes tumor growth and chemoresistance by dysregulating apoptosis and autophagy.
TIPRL antibodies, typically polyclonal or monoclonal reagents raised against specific epitopes (e.g., human TIPRL residues), are essential tools for detecting TIPRL expression in tissues or cell lines via Western blotting, immunoprecipitation, or immunofluorescence. They aid in elucidating TIPRL’s role in mTOR pathway regulation, cancer biology, and therapeutic targeting. Recent research also explores TIPRL’s involvement in viral infections and neurological disorders, highlighting its broad functional relevance. Validated antibodies with high specificity are critical, as TIPRL shares homology with other phosphatases. Commercial antibodies often target conserved regions (e.g., C-terminal domains) and are tested for cross-reactivity across species (human, mouse, rat).