ANGPTL3 Human

ANGPTL3 contains an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain. This protein is involved in the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins . It has been observed that loss-of-function mutations in ANGPTL3 result in a distinct phenotype called familial combined hypolipidemia, characterized by low plasma triglyceride, low-density lipoprotein (LDL), and high-density lipoprotein (HDL) cholesterol concentrations .

Inhibition of ANGPTL3 by a monoclonal antibody has been shown to reduce plasma LDL cholesterol concentrations by up to 50% in healthy volunteers as well as in patients with homozygous familial hypercholesterolemia . This makes ANGPTL3 a potential target for therapeutic interventions aimed at managing cholesterol levels and associated cardiovascular risks.

Recombinant human ANGPTL3 is produced using various expression systems, including baculovirus-infected insect cells and Chinese Hamster Ovary (CHO) cells . The recombinant protein is often tagged with histidine for purification purposes and is available in carrier-free formulations to avoid interference in experimental applications .

Recombinant ANGPTL3 is used in research to study its role in lipid metabolism and its potential as a therapeutic target. It is also used in assays to measure its ability to inhibit lipoprotein lipase activity, which is crucial for understanding its function in lipid regulation .

The recombinant protein is typically lyophilized and should be reconstituted in sterile PBS. It is stable for up to 12 months when stored at -20 to -70°C and should be handled to avoid repeated freeze-thaw cycles .

ANGPTL3 continues to be a significant focus of research due to its crucial role in lipid metabolism and potential therapeutic applications.