Human PLRP2 qPCR Primer Pair

Protein Function: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:19451396, PubMed:20083229, PubMed:21865348, PubMed:26494624). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (PubMed:19824014, PubMed:21652702, PubMed:23732775). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:21652702, PubMed:21865348). Can completely deacylate triacylglycerols (PubMed:21865348). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:20083229, PubMed:26494624). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:18702514, PubMed:20083229). May act together with LIPF to hydrolyze partially digested triglycerides (PubMed:23732775). Hydrolyzes long-chain monoglycerides with high efficiency (PubMed:17401110, PubMed:21652702, PubMed:23732775). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (PubMed:17401110, PubMed:18702514). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity) [The Uniprot Consortium]