PAF Acetylhydrolase 2 (human, recombinant)

HSD-PLA2|PAF-AH2|Platelet-Activating Factor Acetylhydrolase 2, Cytoplasmic|Serine-Dependent Phospholipase A2

PAF acetylhydrolase 2 (PAF-AH2) is a serine-dependent, intracellular-type platelet-activating factor (PAF) acetylhydrolase that is expressed in a variety of tissue and cell types but is most abundant in the liver, kidney, testis, and intestines.{7103,42493,42494,42495} It contains an N-terminal myristoylation site and can translocate from the cytosol to cellular membranes in response to various stressors including UVB radiation, LPS, or oxidative stress, during which PAF-AH2 localizes to the endoplasmic reticulum and Golgi apparatus.{42493,5537} PAF-AH2 hydrolyzes and inactivates PAF, a phospholipid mediator involved in a variety of biological activities, including inflammation, smooth muscle contraction, and fetal development.{42493,42494,6501} It also hydrolyzes phospholipids with short-chain or oxidized fatty acids at the sn-2 position.{7103,42493} PAF-AH2 has demonstrated protective activities in various in vitro and in vivo models of oxidative stress.{42493,42495,5537} Overexpression of PAF-AH2 reduces cytotoxicity and apoptosis induced by tert-butylhydroperoxide (t-BuOOH) in CHO-K1 cells.{5537} Conversely, PAF-AH2-deficient (Pafah2-/-) mouse embryonic fibroblasts (MEFs) are more susceptible to t-BuOOH-induced cell death than wild-type MEFs.{42495} In addition, Pafah2-/- mice exhibit increased hepatic necrosis compared to wild-type animals in a mouse model of carbon tetrachloride-induced hepatic injury.

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≥80% estimated by SDS page