Reactivity | MuSpecies Glossary |
Applications | Inhibition Activity |
Format | Carrier-Free |
Details of Functionality | 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 2.5‑12.5 µg/mL. |
Source | Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse Angiopoietin-like Protein 3/ANGPTL3 protein Ser17-Thr455, with a C-terminal 10-His tag |
Accession # | |
N-terminal Sequence | Ser17 |
Structure / Form | Oligomer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Angptl3 |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 51.8 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. |
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SDS-PAGE | 60 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS, NaCl and CHAPS. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Angiopoietin-like 3 (ANGPTL3) is a secreted glycoprotein that is structurally related to the angiopoietins (1-3). Mature mouse ANGPTL3 contains an N-terminal coiled-coil domain and a C‑terminal fibrinogen-like domain (4). ANGPTL3 is expressed in the liver from early in development through adulthood (4, 5). Full length ANGPTL3 circulates in the plasma as do the proteolytically separated N- and C‑terminal fragments containing the coiled‑coil domain and fibrinogen-like domains, respectively (6, 7). ANGPTL3 is found as 70 kDa, 50 kDa, and 32 kDa species and can form weakly associated noncovalent multimers in vitro (5, 6). ANGPTL3 directly inhibits lipoprotein lipase (LPL), an enzyme responsible for hydrolyzing circulating triglycerides (8). This activity requires a putative heparin-binding motif that is N-terminal to the coiled-coil domain (6). Proteolytic removal of the fibrinogen-like domain from the N-terminal fragment serves to activate ANGPTL3 and increase its ability to inhibit LPL in vitro and function in vivo (6). ANGPTL3 promotes an increase in circulating triglyceride levels without altering VLDL or HDL secretion or uptake (6-8). ANGPTL3 knockout mice are hypolipidemic and have elevated LPL activity (9). ANGPTL3 expression in vivo is upregulated by LXR agonists and downregulated by insulin, leptin, and TR beta agonists (10-12). Dysregulated ANGPTL3 expression and elevated plasma triglyceride levels are characteristic of some strains of obese and diabetic mice, (7, 8, 11). ANGPTL3 does not bind Tie-1 or Tie-2 but its fibrinogen-like domain interacts with integrin alpha V beta 3 to induce endothelial cell adhesion, migration, and neovascularization (13). ANGPTL3, secreted by fetal liver cells, also promotes the expansion of hematopoietic stem cells (14). Mature mouse ANGPTL3 shares 22%-30% amino acid (aa) sequence identity with ANGPTL1, 2, 4, 6, and 7. It shares 77% aa sequence identity with human ANGPTL3.
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