| Description: | PLA2G16 Protein, with dual functionality, acts as a phospholipase exhibiting calcium-independent PLA1 and PLA2 activities, preferentially releasing fatty acids through PLA1. It also serves as an O-acyltransferase and N-acyltransferase, contributing to the formation of N-acylphosphatidylethanolamine, a precursor for N-acylethanolamines. Beyond lipid modification, PLA2G16 is crucial in eye lens differentiation, promoting organelle rupture. In microbial infections, it aids picornaviruses, facilitating genome release and sensing membrane damage at entry sites. PLA2G16's diverse functions highlight its roles in cellular and infection-related processes. PLA2G16 Protein, Human (His) is the recombinant human-derived PLA2G16 protein, expressed by E. coli, with N-6*His labeled tag. The total length of PLA2G16 Protein, Human (His) is 121 a.a., with molecular weight of 14-17 kDa. |
