Mouse Angiopoietin-like Protein 4/ANGPTL4 Antibody New
Mouse Angiopoietin-like Protein 4/ANGPTL4 Antibody Summary
Accession # Q9Z1P8
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Angiopoietin-like Protein 4/ANGPTL4
Angiopoietin-like 4 (ANGPTL4), also known as FIAF, FARP, and PGAR, is a 55 kDa glycoprotein secreted by the liver and fat tissue. It is structurally related to the angoipoietins and contains an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain which can be proteolytically separated in vivo (1). Mature mouse ANGPTL4 shares 26%-30% amino acid (aa) sequence identity with mouse ANGPTL1, 2, 3, 4, 6, and 7. It shares 75% and 97% aa sequence identity with human and rat ANGPTL4, respectively. The coiled coil domain, which is not glycosylated, mediates the formation of variable sized disulfide-linked oligomers (2). This domain directly inhibits lipoprotein lipase, resulting in increased circulating triglyceride levels (3, 4). In humans, the N-terminal fragment and full length ANGPTL4 physically associate with HDL (4). In mouse, however, full length ANGPTL4 associates with HDL, while the N-terminal fragment associates with LDL (4). Circulating ANGPTL4 is decreased in type II diabetics with a subsequent loss of its normal plasma glucose lowering activity (5). Its expression in adipose tissue is induced by fasting and suppressed by feeding (6). In hypoxic areas, ANGPTL4 is induced in both vascular endothelial cells and tumor cells (7, 8). The N-terminal fragment can function as an angiogenesis inhibitor (7, 8). In contrast, the C-terminal fragment modulates cell adhesion through interactions with heparan sulfate proteoglycans, Integrins beta 1 and beta 5, Vitronectin, and Fibronectin, thereby promoting keratinocyte migration and wound healing (7, 9, 10). ANGPTL4 additionally enhances the survival of hematopoietic and mesenchymal stem cells (11, 12). The expression of an undersialylated form of ANGPTL4 in renal podocytes contributes to proteinuria and nephrotic syndrome (13).
- Zhu, P. et al. (2012) Biosci. Rep. 32:211.
- Ge, H. et al. (2004) J. Biol. Chem. 279:2038.
- Sukonina, V. et al. (2006) Proc. Natl. Acad. Sci. USA 103:17450.
- Mandard, S. et al. (2006) J. Biol. Chem. 281:934.
- Xu, A. et al. (2005) Proc. Natl. Acad. Sci. USA 102:6086.
- Kersten, S. et al. (2000) J. Biol. Chem. 275:28488.
- Cazes, A. et al. (2006) Circ. Res. 99:1207.
- Le Jan, S. et al. (2003) Am. J. Pathol. 162:1521.
- Goh, Y.Y. et al. (2010) Am. J. Pathol. 177:2791.
- Goh, Y.Y. et al. (2010) J. Biol. Chem. 285:32999.
- Blank, U. et al. (2012) Eur. J. Haematol. 89:198.
- Hou, M. et al. (2014) PLoS ONE 9:e85808.
- Clement, L.C. et al. (2011) Nat. Med. 17:117.
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