Recombinant Mouse Angiopoietin-like 3 (HA-Tag) Protein, CF Summary
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 (Catalog # 9888-LL)
is present at 0.5 μg/mL, and p‑nitrophenyl butyrate concentration is 1
mM in 0.1 M sodium phosphate, 0.15 M NaCl, 0.5% Triton® X-100, pH 7.2,
is 2-10 µg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse Angiopoietin-like Protein 3/ANGPTL3 protein Hemagglutinin Tag (YPYDVPDYA)
| Mouse Angiopoietin-like Protein 3 (Ser17-Thr455) Accession # Q9R182
| N-terminus | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Tyr
|
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
52 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 |
59-71 kDa and 33-38 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
- 12 months from date of receipt, ≤ -20 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, ≤ -20 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS, NaCl and CHAPS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 400 μg/mL in water. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Angiopoietin-like 3 (HA-Tag) Protein, CF
Background
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 up‑regulated by LXR agonists and down-regulated 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.
- Li, C. (2006) Curr. Opin. Lipidol. 17:152.
- Oike, Y. et al. (2004) Int. J. Hematol. 80:21.
- Kersten, S. (2005) Biochem. Soc. Transact. 33:1059.
- Conklin, D. et al. (1999) Genomics 62:477.
- Ge, H. et al. (2005) J. Lipid Res. 46:1484.
- Ono, M. et al. (2003) J. Biol. Chem. 278:41804.
- Koishi, R. et al. (2002) Nat. Genet. 30:151.
- Shimizugawa, T. et al. (2002) J. Biol. Chem. 277:33742.
- Koster, A. et al. (2005) Endocrinology 146:4943.
- Inaba, T. et al. (2003) J. Biol. Chem. 278:21344.
- Shimamura, M. et al. (2004) Biochem. Biophys. Res. Commun. 322:1080.
- Fugier, C. et al. (2006) J. Biol. Chem. 281:11553.
- Camenisch, G. et al. (2002) J. Biol. Chem. 277:17281.
- Zhang, C.C. et al. (2006) Nat. Med. 12:240.
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