Anti-ANGPTL3 Antibody Picoband® Fluoro488 Conjugated

ANGPTL3 (Angiopoietin-Like 3), also known as ANGPT5, is a protein which in humans is encoded by the ANGPTL3 gene. The protein encoded by this gene is a member of the angiopoietin-like family of secreted factors. By radiation hybrid mapping and the use of surrounding genes, this gene is mapped to chromosome 1p31. It is predominantly expressed in the liver, and has the characteristic structure of angiopoietins, consisting of a signal peptide, N-terminal coiled-coil domain and the C-terminal fibrinogen (FBN) -like domain. Angptl3 also acts as dual inhibitor of lipoprotein lipase (LPL) and endothelial lipase (EL), and increases plasma triglyceride and HDL cholesterol in rodents. ANGPTL3 inhibit endothelial lipase to catalyze HDL-phospholipid and increase HDL-PL levels.

Angiopoietin-related protein 3; Angiopoietin-5; ANG-5; Angiopoietin-like protein 3; ANGPTL3 (17-221) ; ANGPTL3 (17-224) ; ANGPTL3; ANGPT5; UNQ153/PRO179

Expressed principally in liver. Weakly expressed in kidney. Binds to adipocytes. Increased expression and colocalization with activated ITGB3 in glomeruli of patients with nephrotic syndrome showing effaced podocyte foot processes (at protein level) .

Angiogenesis, Cancer, Cardiovascular, Energy Metabolism, Energy Transfer Pathways, Growth Factors, Lipid Metabolism, Metabolic Signaling Pathways, Metabolism, Obesity, Pathways and Processes, Signal Transduction

Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism (PubMed:11788823, PubMed:12909640, PubMed:23661675, PubMed:25495645) . Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity) . Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an in mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1 (PubMed:12097324, PubMed:19318355, PubMed:20581395) . Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids (PubMed:17110602, PubMed:19028676) . Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (PubMed:12565906) . Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL) -TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity) . Contributes to lower plasma levels of low density lipoprotein (LDL) -cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity) .

1. Camenisch, G, Pisabarro, M. T., Sherman, D., Kowalski, J., Nagel, M., Hass, P, Xie, M.-H., Gurney, A., Bodary, S., Liang, X. H., Clark, K., Beresini, M, Ferrara, N., Gerber, H.-P. ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha-v-beta-3 and induces blood vessel formation in vivo. J. Biol. Chem. 277: 17281-17290, 2002. 2. Conklin, D., Gilbertson, D., Taft, D. W., Maurer, M. F., Whitmore, T. E., Smith, D. L., Walker, K. M., Chen, L. H., Wattler, S., Nehls, M., Lewis, K. B. Identification of a mammalian angiopoietin-related protein expressed specifically in liver. Genomics 62: 477-482, 1999. 3. Koishi, R., Ando, Y., Ono, M., Shimamura, M., Yasumo, H., Fujiwara, T., Horikoshi, H., Furukawa, H. Angptl3 regulates lipid metabolism in mice. Nature Genet. 30: 151-157, 2002.