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 . Mature human ANGPTL4 shares 26%-30% amino acid (aa) sequence identity with ANGPTL1, 2, 3, 5, 6, and 7. The coiled coil domain, which is not glycosylated, mediates the formation of variable sized disulfide-linked oligomers . This domain directly inhibits lipoprotein lipase, resulting in increased circulating triglyceride levels. In humans, the N-terminal fragment and full length ANGPTL4 physically associate with HDL. In mouse, however, full length ANGPTL4 associates with HDL, while the N-terminal fragment associates with LDL. Circulating ANGPTL4 is decreased in type II diabetics with a subsequent loss of its normal plasma glucose lowering activity. Its expression in adipose tissue is induced by fasting and suppressed by feeding. In hypoxic areas, ANGPTL4 is induced in both vascular endothelial cells and tumor cells. The N-terminal fragment can function as an angiogenesis inhibitor. 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. ANGPTL4 additionally enhances the survival of hematopoietic and mesenchymal stem cells . The expression of an undersialylated form of ANGPTL4 in renal podocytes contributes to proteinuria and nephrotic syndrome.

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-25 ~ -15℃保存，收到货之后有效期1年。 复溶后， 无菌条件下，-85 ~ -65℃保存，3个月有效期。