Mouse Angiopoietin-like 3 (aa 17-220) Biotin組換え体(リコンビナント)タンパク質 | Recombinant Mouse Angiopoietin-like 3 (aa 17-220) Biotin

R&D Systems社の高品質なMouse Angiopoietin-like 3 (aa 17-220) Biotinの組換え体タンパク質(Recombinant Mouse Angiopoietin-like 3 (aa 17-220) Biotin)です。

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R&D Systems社組換え体タンパク質製品では通常ウシ血清アルブミン(BSA)をキャリアタンパク質として加えています。キャリアタンパク質を加えることで組換え体タンパク質の安定性が高まり、使用期限が長くなります。また、より濃度の低い溶液での保管も可能となります。CF製品はBSAが含まれない製品となります。一般的に細胞培養や、ELISAのスタンダードにはBSA含有製品を推奨しています。CF製品はBSAが影響してしまうアプリケーションに推奨されます。

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 separatedN- 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).