PLRP2 Protein, Human (sf9, His)

The PLRP2 protein is a multifunctional lipase that hydrolyzes triglycerides and galactosylglycerides with broad substrate specificity. It is essential for newborns and plays an important role in the pancreas' digestion of dietary fats, especially milk fat globules, which are rich in long-chain triglycerides. PLRP2 Protein, Human (sf9, His) is the recombinant human-derived PLRP2 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of PLRP2 Protein, Human (sf9, His) is 469 a.a., with molecular weight of ~57 kDa.

PLRP2, a versatile lipase, is a key player in the hydrolysis of triglycerides and galactosylglycerides, exhibiting broad substrate specificity without apparent positional preferences. Particularly crucial in neonates, PLRP2 plays a major role in pancreatic digestion of dietary fats, such as milk fat globules enriched in long-chain triglycerides. As the liver matures and bile salt synthesis increases, PLRP2 likely functions primarily as a galactolipase and monoacylglycerol lipase, efficiently hydrolyzing monogalactosyldiglycerols and digalactosyldiacylglycerols present in plant-based diets. In collaboration with LIPF, PLRP2 contributes to the hydrolysis of partially digested triglycerides. Additionally, in cytotoxic T cells, PLRP2 contributes to perforin-dependent cell lysis, while also exhibiting low phospholipase activity. In neurons, PLRP2 plays a crucial role in the localization of specific phospholipids to neurite tips, facilitating the surface expression of the dopamine transporter SLC6A3/DAT through intricate membrane domain remodeling and vesicle fusion events.

Human

Sf9 insect cells

C-His

P54317 (M1-C469)

5408  [NCBI]

Approximately 57 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.