Anti-Human Lipoprotein Lipase Antibody Pair

Product Description: Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism, responsible for hydrolyzing triglycerides in circulating lipoproteins, such as chylomicrons and very low-density lipoproteins (VLDL), into free fatty acids and monoacylglycerol. This process provides energy substrates for tissues like adipose, skeletal muscle, and the heart. LPL functions as a non-covalent homodimer and requires ApoC-II as a cofactor for activation. It is anchored to the endothelial surface via glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1). Structurally, LPL contains an N-terminal alpha/beta hydrolase domain with a catalytic triad (Ser159, Asp183, His268) and a C-terminal beta-barrel domain that determines substrate specificity. These domains are connected by a hinge region critical for enzymatic activity. Mutations or deficiencies in LPL can lead to familial chylomicronemia syndrome (FCS), characterized by severe hypertriglyceridemia, pancreatitis, and lipid deposition disorders. Dysregulated LPL activity has also been implicated in obesity, diabetes, and cardiovascular diseases. Protein Function: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:11342582, PubMed:27578112, PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:12032167, PubMed:7592706). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232) [The Uniprot Consortium]