PLA2G7 Protein, Human (HEK293, His)

Platelet-activating factor acetylhydrolase (PLA2G7) is a lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress responses. At the lipid-aqueous interface, PLA2G7 hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids, that specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position. It also hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory signaling lipid that acts through PTAFR on various innate immune cells. In addition, PLA2G7 hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in low-density lipoprotein (LDL) particles and uncontrolled pro-inflammatory effects. As part of high-density lipoprotein (HDL) particles, PLA2G7 can hydrolyze phospholipids having long-chain fatty acyl hydroperoxides at sn-2 position and protect against potential accumulation of these oxylipins in the vascular wall. PLA2G7 catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage^{[1][2][3][4][5]}.