PLA2G1B Protein, Human (HEK293, His)

The PLA2G1B protein is a secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. It hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids, with a preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. This protein may play a role in the biosynthesis of N-acyl ethanolamines, which regulate energy metabolism and inflammation in the intestinal tract. It also hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. It may act in an autocrine and paracrine manner and, when bound to the PLA2R1 receptor, can regulate podocyte survival and glomerular homeostasis. Additionally, PLA2G1B has anti-helminth activity, which is regulated by the gut microbiota. Upon helminth infection of intestinal epithelia, it directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, potentially controlling processes such as membrane fusion and cell division while aiding in immune recognition. This ultimately reduces larvae integrity and infectivity.