Recombinant Human Angiopoietin-like 4 C-Terminal Frag, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Angiopoietin‑like 4/ANGPTL4 C‑Terminal Fragment is immobilized at 1 μg/mL, 100 μL/well, the concentration of Recombinant Human LILRB2/CD85d/ILT4 Fc Chimera
(Catalog #
2078-T4) binds with an ED50 of 70.0-350 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Angiopoietin-like Protein 4/ANGPTL4 protein Leu165-Ser406, with a C-terminal 6-His tag
>90%, 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
28 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
36 kDa, reducing conditions
Publications
Read Publications using 3485-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 Tris-Citrate and NaCl.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 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 Human Angiopoietin-like 4 C-Terminal Frag, 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
ANGPT-L4, also known as FIAF, FARP, and PGAR, is a 55 kDa glycoprotein secreted by the liver and fat tissue that is structurally related to the angiopoietins. It contains an N‑terminal coiled coil domain and a C‑terminal fibrinogen-like domain which can be proteolytically separated in vivo (1, 2). Mature human ANGPT‑L4 shares 26%‑30% amino acid (aa) sequence identity with ANGPT-L1, 2, 3, 5, 6, and 7. It shares approximately 75% aa sequence identity with mouse and rat ANGPT‑L4. The coiled coil domain, which is not glycosylated, mediates the formation of variable sized disulfide-linked oligomers (3, 4). This domain directly inhibits lipoprotein lipase, resulting in increased circulating triglyceride levels (5-9). In human, the N-terminal fragment and full length ANGPT-L4 physically associate with HDL (9). In mouse, however, full length ANGPT-L4 associates with HDL, while the N-terminal fragment associates with LDL (9). Circulating ANGPT-L4 is decreased in type II diabetics with a subsequent loss of its normal plasma glucose lowering activity (10). Its expression in adipose tissue is induced by fasting and suppressed by feeding (3, 11). Its expression in both liver and fat is up‑regulated by PPAR alpha , beta , gamma , and δ agonists and down‑regulated by insulin (3, 12, 13). ANGPT-L4 is induced in vascular endothelial cells by hypoxia and in hypoxic areas surrounding tumors (14-16). The full length molecule but not the C-terminal fragment is bound by heparan sulfate proteoglycans and functions as an angiogenesis inhibitor (14, 15).
Li, C. (2006) Curr. Opin. Lipidol. 17:152.
Kersten, S. (2005) Biochem. Soc. Transact. 33:1059.
Ge, H. et al. (2005) J. Lipid Res. 46:1484.
Ge, H. et al. (2004) J. Biol. Chem. 279:2038.
Sukonina, V. et al. (2006) Proc. Natl. Acad. Sci. 103:17450.
Koster, A. et al. (2005) Endocrinology 146:4943.
Yoshida, K. et al. (2002) J. Lipid Res. 43:1770.
Ge, H. et al. (2004) J. Lipid Res. 45:2071.
Mandard, S. et al. (2006) J. Biol. Chem. 281:934.
Xu, A. et al. (2005) Proc. Natl. Acad. Sci. 102:6086.
Kersten, S. et al. (2000) J. Biol. Chem. 275:28488.
Mandard, S. et al. (2004) J. Biol. Chem. 279:34411.
Yamada, T. et al. (2006) Biochem. Biophys. Res. Commun. 347:1138.
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