PAF Acetylhydrolase 2 (human, recombinant)

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. 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. PAF-AH2 hydrolyzes and inactivates PAF, a phospholipid mediator involved in a variety of biological activities, including inflammation, smooth muscle contraction, and fetal development. It also hydrolyzes phospholipids with short-chain or oxidized fatty acids at the sn-2 position. PAF-AH2 has demonstrated protective activities in various in vitro and in vivo models of oxidative stress. Overexpression of PAF-AH2 reduces cytotoxicity and apoptosis induced by tert-butylhydroperoxide (t-BuOOH) in CHO-K1 cells. Conversely, PAF-AH2-deficient (Pafah2-/-) mouse embryonic fibroblasts (MEFs) are more susceptible to t-BuOOH-induced cell death than wild-type MEFs. In addition, Pafah2-/- mice exhibit increased hepatic necrosis compared to wild-type animals in a mouse model of carbon tetrachloride-induced hepatic injury.Synonyms: PAF-AH2, HSD-PLA2, Platelet-Activating Factor Acetylhydrolase 2, Cytoplasmic, Serine-Dependent Phospholipase A2. Purity: >80% estimated by SDS page. Source: Active recombinant N-terminal His-tagged protein expressed in E. coli. Amino Acids: 2-392. MW: 46.1 kDa. Storage Buffer: 50 mM HEPES, pH 8.0, with 300 mM sodium chloride and 20% glycerol. UniProt Accession #: Q99487.