Measured by its ability to inhibit lipoprotein lipase activity. Yoshida, K. et al. (2002) J. Lipid Res. 43:1770. The IC50 value under conditions in which Recombinant Human Lipoprotein Lipase/LPL
(Catalog #
9888-LL)
and p-nitrophenyl butyrate are present in 0.1 M sodium phosphate, 0.15 M NaCl, 0.5% Triton® X-100, pH 7.2, is approximately 0.1‑1 µg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Angiopoietin-like Protein 4/ANGPTL4 protein Gln24-Ser410, with a C-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Inhibition Activity
Theoretical MW
44.2 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
55-65 kDa, reducing conditions
Publications
Read Publications using 4880-AN in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS and NaCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Angiopoietin-like 4 Protein, CF
Angiopoietin like Protein 4
angiopoietin-like 4
Angiopoietin-like Protein 4
ANGPTL4
ARP4fasting-induced adipose factor
FIAF
FIAFhepatic angiopoietin-related protein
Hepatic fibrinogen/angiopoietin-related protein
HFARP
HFARPANGPTL2
NL2
peroxisome proliferator-activated receptor (PPAR) gamma inducedangiopoietin-related protein
PGAR
PGARangiopoietin-related protein 4
pp1158
PPARG angiopoietin related protein
Background
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.
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