Lipid modifications include Glycosyl-phosphatidylinositol anchor (GPI). At the C-terminus of proteins, it happens in the endoplasmic reticulum that the post-translational linkage between glycosylphosphatidylinositol and the modified proteins are translocated to the membrane, which are remain anchored to the outer leaflet of the cell membrane. Methods for detecting protein lipidation have been exploited to predict GPI-anchored proteins, N-myristoylated, S-isoprenylated or S-palmitoylated proteins, and so on. The traditional approaches are based on the incorporation of radioactive precursors and subsequent detection of the proteins by fluorography. Mass spectrometry (MS) methods are universally applied, which are for the mapping of post-translational modifications. This technology submits crucial advantages. Bio-orthogonal probes, reactions compatible with biomolecules that allow their study in their native settings. https://www.creative-proteomics.com/pronalyse/lipidation-analysis.html