Cayman PLA2 (human, recombinant Group XV), 25 µg

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Phospholipase A₂ (PLA₂) (Group XV), also known as lysosomal phospholipase A and acetyltransferase, is a calcium-independent and acidic pH-optimum phospholipase encoded by PLA2G15 in humans.^1,2 It is composed of an α/β-hydrolase domain, a cap domain, and a membrane-binding domain, is ubiquitously expressed, and localizes to lysosomes.^1,3 PLA2 (Group XV) hydrolyzes sn-1 and sn-2 fatty acids in phospholipids, contributing to phospholipid degradation in lysosomes.¹ It also functions as a bis(monoacylglycerol) phosphate (BMP) hydrolase, hydrolyzing BMP lipid species independent of their saturation or chain length.⁴ Pla2g15 knockdown induces phospholipidosis and enlargement of alveolar macrophages, mimicking a foam cell phenotype, in young mice. In aged mice, Pla2g15 knockdown induces the development of glomerulonephritis, lymphoid hypertrophy, and abnormal serologies, including positive anti-nuclear antibodies, anti-dsDNA antibodies, and high circulating immunoglobulin levels, indicating an autoimmune phenotype similar to systemic lupus erythematosus (SLE). Similar to PLA2G15 knockout, pharmacologic inhibition of PLA₂ (Group XV) by cationic amphiphilic drugs, such as amiodarone, induces phospholipidosis in cells, indicating that PLA₂ (Group XV) may be a screening candidate for prediction of drug-induced phospholipidosis during pre-clinical drug development studies.⁵ Pla2g15 knockdown reduces Purkinje cell loss, microgliosis, astrocytosis, and CNS demyelination in a mouse model of Niemann-Pick disease type C1 (NPC1).⁴ Cayman’s PLA₂ (human, recombinant Group XV) can be used for enzyme activity assay and Western blot (WB) applications.

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