Anti-PLA2G1B

Protein function: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:1420353, PubMed:10681567, PubMed:17603006). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:1420353, PubMed:10681567, PubMed:17603006). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. May act in an autocrine and paracrine manner (PubMed:7721806, PubMed:25335547). Upon binding to the PLA2R1 receptor can regulate podocyte survival and glomerular homeostasis (PubMed:25335547). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity. [The UniProt Consortium] Buffer: 40% glycerol and PBS (pH 7.2). 0.02% sodium azide is added as preservative. Highest antigen sequence identity to mouse: 79% and to rat: 77%