Recombinant Cynomolgus Angiopoietin-like 3 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 for this effect is 1.5-9 μg/mL.
|
Source |
Trichoplusia ni, T. ni (baculovirus)-derived cynomolgus monkey Angiopoietin-like Protein 3/ANGPTL3 protein Ser17-Glu460, with a C-terminal 10-His tag |
Accession # |
|
N-terminal Sequence |
Ser17 |
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 |
53 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 |
56-65 kDa, reducing conditions
|
Packaging, Storage & Formulations
Storage |
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 °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 250 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 Cynomolgus Angiopoietin-like 3 Protein, CF
Background
ANGPTL3 is a secreted glycoprotein that is structurally
related to the Angiopoietins (1-3). Mature 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 proteolytically separated N- and
C-terminal fragments containing the coiled‑coil domain and fibrinogen-like
domains, respectively (6, 7).ANGPTL3 directly inhibits lipoprotein lipase (LPL) and endothelial lipase (EL),
enzymes responsible for hydrolyzing circulating triglycerides and HDL
phospholipids (8, 9). This activity requires a putative heparin-binding
motif which 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 (10).
ANGPTL3 expression
in vivo is up-regulated by LXR agonists and down-regulated
by insulin, leptin, and agonists of TR beta or PPAR beta (11-14). Dysregulated
ANGPTL3 expression and elevated plasma triglyceride levels are characteristic
of some strains of obese and diabetic mice (7, 8, 12). ANGPTL3 does not bind
Tie1 or Tie2, but its fibrinogen-like domain interacts with integrin alpha V beta 3 to induce endothelial cell adhesion, migration, and neovascularization
(15). ANGPTL3, secreted by fetal liver, also promotes the expansion of
hematopoietic stem cells (16). Mature Cynomolgus Monkey ANGPTL3 shares 97%, 77%,
and 78% amino acid sequence identity with human, mouse, and rat ANGPTL3, respectively.
- Li, C. (2006) Curr. Opin. Lipidol. 17:152.
- Oike, Y. et al. (2004) Int. J. Hematol. 80:21.
- Kersten, S. (2005) Biochem. Soc. Trans. 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.
- Shimamura, M. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:366.
- 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.
- Matsusue, K. et al. (2006) Mol. Cell Endocrinol. 256:23.
- Camenisch, G. et al. (2002) J. Biol. Chem. 277:17281.
- Zhang, C.C. et al. (2006) Nat. Med. 12:240.
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