Recombinant Human Angiopoietin-like 3 (aa 17-220), CF
Recombinant Human Angiopoietin-like 3 (aa 17-220), CF Summary
Product Specifications
Ser17-Pro220, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
4954-AN
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and NaCl. |
| Reconstitution | Reconstitute at 200 μg/mL in sterile PBS. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Angiopoietin-like Protein 3/ANGPTL3
Angiopoietin-like 3 (ANGPTL3) is a secreted glycoprotein that is structurally related to the angiopoietins (1-3). Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain (4). Within the N-terminal region, human ANGPTL3 shares 15%-21% amino acid (aa) sequence identity with ANGPTL1, 2, 4, 5, 6, and 7, and 82% with mouse and rat ANGPTL3. 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 segments 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) 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 cells, also promotes the expansion of hematopoietic stem cells (16).
- 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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