Recombinant Cynomolgus Angiopoietin-like 3 Protein, CF Summary
Ser17-Glu460, with a C-terminal 10-His tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS, NaCl and CHAPS with Trehalose.|
|Reconstitution||Reconstitute at 250 μg/mL in water.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Recombinant Cynomolgus Monkey Angiopoietin‑likeProtein 3/ANGPTL3 (Catalog # 10052-AN) dose dependently inhibits RecombinantHumam LPL (Catalog # 9888-LL) activity with an IC50 of 1.5-9 μg/mL.
2 μg/lane of Recombinant Cynomolgus Monkey Angiopoietin‑like Protein 3/ANGPTL3 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 56-65 kDa.
Background: Angiopoietin-like Protein 3/ANGPTL3
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.
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