Recombinant Mouse Angiopoietin-like 3 (aa 17-220) Biotin, CF Summary
Ser17-Thr206, with a C-terminal 6-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 MOPS, NaCl and CHAPS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|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.
Both Biotinylated rmANGPTL3 (Catalog # BT8344) and unlabeled rmANGPTL3 (Catalog # 8344-AN) stimulate the expansion of E16-E18 rat liver mononuclear cells link, in the presence of rmSCF (Catalog # 455-MC), rmTpo (Catalog # 488-TO), and rmFlt-3L (Catalog # 427-FL). The ED50for this effect is 20-120 ng/mL in the presence of a cross-linking antibody, His Tag MAb (Catalog # MAB050). The similarity in activity highlights that the biotinylated protein is fully functional.
Background: Angiopoietin-like Protein 3/ANGPTL3
Angiopoietin-like Protein 3 (ANGPTL3) is a secreted glycoprotein that is structurally related to the angiopoietins (1). Mature mouse ANGPTL3 contains an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain (2). Mature mouse ANGPTL3 shares 77% aa sequence identity with human ANGPTL3. ANGPTL3 is expressed in the liver from early in development through adulthood (2, 3). 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 (4, 5). The cleavage of ANGPTL3 by Furin and Proprotein Convertase 5/6 is enhanced by its interaction with the related ANGPTL8 (6, 7). ANGPTL3 is found as 70 kDa, 50 kDa, and 32 kDa species and can form weakly associated noncovalent multimers in vitro (3, 4). 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 (4). 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 [Ono 41804]. ANGPTL3 promotes an increase in circulating triglyceride levels without altering VLDL or HDL secretion or uptake (4, 5, 8). ANGPTL3 knockout mice are hypolipidemic and have elevated LPL activity (10). ANGPTL3 expression in vivo is upregulated by LXR agonists and downregulated 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 (5, 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).
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