LIPG Human

Lipase Endothelial (Human Recombinant) is produced in HEK (Human Embryonic Kidney) cells. The recombinant form is a single, glycosylated polypeptide chain consisting of 490 amino acids, with a calculated molecular mass of approximately 55.8 kDa . The enzyme is fused to a 2 amino acid N-terminal linker, a 2 amino acid C-terminal linker, and a 6 amino acid His tag at the C-terminus .

LIPG exhibits extensive phospholipase activity and is more active as a phospholipase than as a triglyceride lipase . It hydrolyzes high-density lipoproteins (HDL) more efficiently than other lipoproteins . This enzyme is involved in the hydrolysis of triglycerides, both with short-chain fatty acyl groups (such as tributyrin) and long-chain fatty acyl groups (such as triolein), showing similar levels of activity toward both types of substrates .

The primary role of LIPG in the body is to regulate lipoprotein metabolism and maintain vascular health. By hydrolyzing HDL, LIPG helps in the remodeling and clearance of plasma lipoproteins . This activity is essential for maintaining lipid homeostasis and preventing the accumulation of lipids in the blood vessels, which can lead to cardiovascular diseases .

Recombinant LIPG is widely used in laboratory research to study its role in lipid metabolism and vascular biology. It is also used to investigate the mechanisms underlying various lipid-related disorders and to develop potential therapeutic interventions .

The lyophilized form of LIPG should be stored at -20°C. After reconstitution, it is recommended to aliquot the product to avoid repeated freezing and thawing cycles. The reconstituted protein can be stored at 4°C for a limited period, typically showing no change after two weeks .