LPL Human, HEK

Lipoprotein Lipase is a glycoprotein that functions as a homodimer. Each monomer consists of 475 amino acids, and the enzyme is heavily glycosylated, which is essential for its stability and function. The recombinant form of human LPL is often expressed in HEK293 cells (Human Embryonic Kidney 293 cells), which provide a suitable environment for proper folding and post-translational modifications .

LPL plays a dual role:

1. Triglyceride Hydrolase Activity: It catalyzes the hydrolysis of triglycerides into free fatty acids and glycerol.
2. Ligand/Bridging Factor: It acts as a ligand or bridging factor for receptor-mediated lipoprotein uptake, facilitating the clearance of triglyceride-rich lipoproteins from the bloodstream .

The enzyme is anchored to the endothelial surface of capillaries in tissues such as the heart, muscle, and adipose tissue through interactions with heparan sulfate proteoglycans. This localization is critical for its function in lipid metabolism .

Mutations in the LPL gene can lead to various lipid metabolism disorders. For instance:

• Type I Hyperlipoproteinemia: This condition results from severe mutations causing LPL deficiency, leading to elevated levels of chylomicrons in the blood.
• Other Lipoprotein Metabolism Disorders: Less severe mutations in LPL are associated with a range of lipid metabolism disorders, impacting cardiovascular health .

The recombinant form of human LPL produced in HEK293 cells is designed to mimic the natural enzyme closely. It is often used in research to study lipid metabolism and related disorders. The recombinant enzyme is typically purified to high levels of purity (>80%) and is biologically active, making it suitable for various biochemical assays .

Recombinant LPL is usually supplied as a lyophilized powder and should be reconstituted in a suitable buffer before use. It is recommended to store the reconstituted enzyme at -20°C to maintain its stability and activity over time .