LIPH
LIPH (lipase H) is a secreted and cell-membrane-associated lipase that hydrolyses phosphatidic acid to produce 2-acyl lysophosphatidic acid (LPA), a bioactive lipid mediator. It is also known as mPA-PLA1, PLA1B, mPA-PLA1alpha and LPDLR. Browse Assay Genie's current range of LIPH research reagents below, or read on for the biology behind the target.
LIPH hydrolyses phosphatidic acid (PA) specifically, releasing a fatty acid and 2-acyl lysophosphatidic acid (LPA). LPA is a potent bioactive lipid mediator. According to NCBI Gene, it has diverse biological properties, including platelet aggregation, smooth muscle contraction, and stimulation of cell proliferation and motility. The enzyme is selective: it does not hydrolyse other phospholipids such as phosphatidylserine, phosphatidylcholine or phosphatidylethanolamine, and it does not act on triacylglycerol.
The LIPH gene encodes a membrane-bound member of the mammalian triglyceride lipase family. The protein belongs to the AB hydrolase superfamily and the lipase family, and it is found both in secreted form and at the cell membrane. This dual localisation is relevant when choosing an approach to study the LIPH protein, whether in cell lysates, membrane fractions or conditioned medium. The mouse and rat orthologs are both named Liph, which allows comparative work across common model species.
The gene is catalogued by HGNC in the lipase gene group under the name lipase H, with the previous name lipase, member H. Aliases such as mPA-PLA1, PLA1B, mPA-PLA1alpha and LPDLR appear in the literature and in databases, so it is worth searching under several names. Because LIPH generates 2-acyl LPA from PA, it is a useful entry point for studying how lipid mediator production is controlled at the cell surface and in the extracellular space.
LIPH produces 2-acyl LPA from phosphatidic acid, making it a key enzyme for studying how this lipid mediator is generated.
LIPH hydrolyses phosphatidic acid but not PS, PC, PE or triacylglycerol, which makes it a clear model of selective lipase activity.
LPA stimulates cell proliferation and motility, so LIPH is of interest wherever LPA-dependent cellular responses are investigated.
LPA is linked to platelet aggregation and smooth muscle contraction, placing LIPH within research on these physiological processes.
LIPH is a lipase that specifically hydrolyses phosphatidic acid, yielding 2-acyl lysophosphatidic acid (LPA) and a fatty acid. It does not hydrolyse phosphatidylserine, phosphatidylcholine, phosphatidylethanolamine or triacylglycerol. The LPA it generates is a potent bioactive lipid mediator.
LIPH stands for lipase H, with the UniProt name lipase member H and the earlier HGNC name lipase, member H. Aliases include mPA-PLA1, PLA1B, mPA-PLA1alpha and LPDLR. Searching under all of these names helps when reviewing the literature on the LIPH gene.
Yes. Both mouse and rat have an ortholog named Liph, so the gene can be studied in common rodent models. Orthologous proteins can differ in sequence, so check the datasheet of any product for its validated reactivity.
Other lipases and lipid-mediator pathway targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8WWY8; product specifications from Assay Genie datasheets.