Recombinant Cynomolgus Angiopoietin-like 3 Protein, CF

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Product Details

Summary
Reactivity Pm-CmSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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

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

  • AGNPT5
  • Ang-5
  • angiopoietin 5
  • Angiopoietin-5
  • angiopoietin-like 3
  • Angiopoietin-like Protein 3
  • angiopoietin-related protein 3
  • ANGPT5angiopoietin-5
  • ANGPTL3
  • FHBL2

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.
  1. Li, C. (2006) Curr. Opin. Lipidol. 17:152.
  2. Oike, Y. et al. (2004) Int. J. Hematol. 80:21.
  3. Kersten, S. (2005) Biochem. Soc. Trans. 33:1059.
  4. Conklin, D. et al. (1999) Genomics 62:477.
  5. Ge, H. et al. (2005) J. Lipid Res. 46:1484.
  6. Ono, M. et al. (2003) J. Biol. Chem. 278:41804.
  7. Koishi, R. et al. (2002) Nat. Genet. 30:151.
  8. Shimizugawa, T. et al. (2002) J. Biol. Chem. 277:33742.
  9. Shimamura, M. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:366.
  10. Koster, A. et al. (2005) Endocrinology 146:4943.
  11. Inaba, T. et al. (2003) J. Biol. Chem. 278:21344.
  12. Shimamura, M. et al. (2004) Biochem. Biophys. Res. Commun. 322:1080.
  13. Fugier, C. et al. (2006) J. Biol. Chem. 281:11553.
  14. Matsusue, K. et al. (2006) Mol. Cell Endocrinol. 256:23.
  15. Camenisch, G. et al. (2002) J. Biol. Chem. 277:17281.
  16. Zhang, C.C. et al. (2006) Nat. Med. 12:240.

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