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Lipid Pull-down is an in vitro affinity purification technique used to systematically identify proteins that interact with specific lipid molecules. In this method, target lipids (e.g., phosphoinositides, sphingolipids, cholesterol) are immobilized on solid-phase supports (such as agarose or magnetic beads) via covalent coupling or biotin-avidin systems. After incubation with cell lysates or tissue extracts, non-specifically bound proteins are removed through washing steps, and specific lipid-interacting proteins are eluted and enriched for subsequent analysis by Western Blot or mass spectrometry. Lipid Pull-down serves as a core tool for investigating lipid signaling, membrane protein recruitment, and lipid raft dynamics. It is widely applied to dissect protein-binding networks of phosphoinositide phosphorylated derivatives, sphingolipid-protein interactions, and cholesterol-associated protein complexes. Combined with quantitative proteomics, this approach enables high-throughput, high-sensitivity screening of lipid-binding proteins.