PLA2G7 Protein, Mouse (sf9, His, Myc)

PLA2G7 protein, a lipoprotein-associated calcium-independent phospholipase A2, plays a pivotal role in phospholipid catabolism during inflammatory and oxidative stress responses. Operating at the lipid-aqueous interface, it hydrolyzes the ester bond of fatty acyl groups at the sn-2 position of phospholipids, with a specific preference for those carrying short-chain fatty acyl groups. Additionally, PLA2G7 can target phospholipids with long fatty acyl chains if they bear oxidized functional groups. The enzyme's versatility extends to inactivating platelet-activating factor (PAF), a potent pro-inflammatory signaling lipid, and hydrolyzing oxidatively truncated phospholipids, preventing their accumulation and uncontrolled pro-inflammatory effects. When associated with high-density lipoprotein (HDL) particles, PLA2G7 contributes to the hydrolysis of phospholipids containing long-chain fatty acyl hydroperoxides, safeguarding against potential oxylipin accumulation in the vascular wall. Furthermore, PLA2G7 catalyzes the release of F2-isoprostanes, serving as lipid biomarkers for cellular oxidative damage.