angptl-3

ANGPTL3 is a secreted glycoprotein that is structurally related to the angiopoietins. Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C‑terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development through adulthood. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. ANGPTL3 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 26.6 kDa and the accession number is Q9Y5C1.

ANGPTL3 is a secreted glycoprotein that is structurally related to the angiopoietins. Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C‑terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development through adulthood. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. ANGPTL3 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 26.6 kDa and the accession number is Q9Y5C1.

Angiopoietin-like 3 (ANGPTL3) is a secreted glycoprotein that is structurally related to the angiopoietins. Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development through adulthood. Full length ANGPTL3 circulates in the plasma as do the proteolytically separated N-and C-terminal segments containing the coiled coil domain and fibrinogen-like domains,respectively. ANGPTL3 directly inhibits lipoprotein lipase (LPL) and endothelial lipase (EL), enzymes responsible for hydrolyzing circulating triglycerides and HDL phospholipids. ANGPTL3 promotes an increase in circulating triglyceride levels without altering VLDL or HDL secretion or uptake. ANGPTL3 expression in vivo is up-regulated by LXR agonists and down-regulated by insulin, leptin, and agonists of TRβ or PPARβ.

Candidates for this common regulatory system include signals mediated by peroxisome proliferator-activated regulator and its response factor, angiopoietin-like 4. The expression and bioactivity of angiopoietin-like 4, an adipocytokine that was originally reported to have an angiogenic function, have been detected not only in the vascular system and adipose tissue but also in rheumatoid joints.