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ANGPTL3 encodes a member of a family of secreted proteins that function in angiogenesis. Additionally we are shipping ANGPTL3 Antibodies (156) and ANGPTL3 Proteins (32) and many more products for this protein.
Showing 10 out of 62 products:
Mouse (Murine) ANGPTL3 ELISA Kit for Sandwich ELISA - ABIN425029
Méndez-González, Julve, Rotllan, Llaverias, Blanco-Vaca, Escolà-Gil: ATP-binding cassette G5/G8 deficiency causes hypertriglyceridemia by affecting multiple metabolic pathways. in Biochimica et biophysica acta 2011
Knockdown of Angptl3 decreases liver size in developing zebrafish.
An ANGPTL3-4-8 model was proposed to explain the variations of lipoprotein lipase (LPL (show LPL ELISA Kits)) activity during the fed-fast cycle. Feeding induces ANGPTL8, activating the ANGPTL8-ANGPTL3 pathway, which inhibits LPL (show LCP1 ELISA Kits) in cardiac and skeletal muscles to direct circulating triglycerides (TG) to white adipose tissue; the reverse is true during fasting, which suppresses ANGPTL8 but induces ANGPTL4 (show ANGPTL4 ELISA Kits), thereby directing TG to muscles.
Inactivation of ANGPTL3 reduces hepatic VLDL-triglyceride secretion
Novel mutation Y344S found in ANGPTL3 gene in two diabetic patients with familial hypobetalipoproteinemia.
Data suggest that silencing of ANGPTL 3 (angiopoietin-like protein 3) improves insulin (show INS ELISA Kits) sensitivity.
HCV core represses ANGPTL-3 expression through loss of HNF-1alpha binding activity and blockage of LXR/RXR transactivation
Data suggest that genetic polymorphisms in ANGPTL3 (angiopoietin-like 3 protein), TIMD4 (show TIMD4 ELISA Kits) (T cell immunoglobulin mucin-4 (show MUC4 ELISA Kits)), and apolipoproteins A5 and B are among the genetic determinants of hypertriglyceridemia in Amerindian populations. [REVIEW]
ANGPTL3 is positively associated with low-density lipoprotein cholesterol and high-density lipoprotein cholesterol and not with metabolic syndrome traits including triglycerides.
Identification of loss-of-function ANGPTL3 mutation is shedding light on a possible role of ANGPTL3 at the crossroads of lipoproteins, fatty acids, and glucose metabolism. [Review]
Although partial Angptl3 deficiency did not affect the activities of lipolytic enzymes, the complete absence of Angptl3 results in an increased lipoprotein lipase (show LPL ELISA Kits) activity and mass and low circulating free fatty acid levels.
No gene-gene interaction was identified other than an interaction between SNPs in the ANGPTL3 and RXRA (show RXRA ELISA Kits) regions, which results in the inhibition of ApoB (show APOB ELISA Kits) reduction in response to statin-FNA therapy.
The deletion of ANGPTL3 tremendously attenuates proteinuria and protects podocytes from injury in a mouse model of adriamycin-induced nephropathy.
ANGPTL3 has a role in regulating white adipose tissue energy homeostasis but not in liver
Data indicate that expression of Angptl3 in hematopoietic stem cell (HSC (show FUT1 ELISA Kits)) through lentiviral transduction promoted HSC (show FUT1 ELISA Kits) expansion.
Angptl3 could induce actin filament rearrangement, mainly in lamellipodia formation, and that this process was mediated by integrin alpha(V)beta-mediated FAK and PI3K phosphorylation and Rac1 activation.
Furin (show FURIN ELISA Kits) has a role as the primary in vivo convertase of ANGPTL3 and endothelial lipase (show LIPG ELISA Kits) in hepatocytes
ANGPTL8, a paralog of ANGPTL3 that arose through duplication of an ancestral DOCK gene, regulates postprandial TAG and fatty acid metabolism by controlling activation of its progenitor, and perhaps other ANGPTLs
Angptl3, as an extrinsic factor, thus supports the stemness of hematopoietic stem cells in the bone marrow niche.
ANGPTL3 expression is upregulated in puromycin-induced podocyte damage and is associated with the reduction of perlecan (show HSPG2 ELISA Kits) and agrin (show AGRN ELISA Kits) expression
a molecular connection between ANGPTL3, lipoprotein lipase (show LPL ELISA Kits), and proprotein convertases
First report of molecular cloning and characterization of ANGPTL3 in pigs, which will be helpful for a better understanding of the role of ANGPTLs in lipid metabolism.
This gene encodes a member of a family of secreted proteins that function in angiogenesis. The encoded protein, which is expressed predominantly in the liver, is further processed into an N-terminal coiled-coil domain-containing chain and a C-terminal fibrinogen chain. The N-terminal chain is important for lipid metablism, while the C-terminal chain may be involved in angiogenesis. Mutations in this gene cause familial hypobetalipoproteinemia type 2.
, WITHDRAWN: zgc:111943
, angiopoietin-related protein 3-like
, angiopoietin 5
, angiopoietin-related protein 3
, angiopoietin-like protein 3