Anti-Lipin 1 antibodies are used in the immunodetection of the protein encoded by the LPIN1 gene. In humans, the canonical protein has a reported length of 890 amino acid residues and a mass of 98.7 kDa. Its subcellular localization is in the nucleus, ER, and cytoplasm. Alternative splicing is reported to yield 7 different isoforms for this protein. It is notably expressed in skeletal muscle. A member of the Lipin protein family, it is known to act as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels. Post-translational modifications have been described, including sumoylation, acetylation and phosphorylation. Other names for this target antigen include PAP1 and phosphatidate phosphatase LPIN1.