ANGPTL4 (fibrinogen-like domain) (human) (rec.)

Angiopoietin-like Protein 4; FIAF; Fasting-induced Adipose Factor; HFARP; Hepatic Fibrinogen/Angiopoietin-related Protein

0.5 mg/ml

32160000

<0.1EU/µg purified protein (LAL test; Lonza).

liquid

Liquid. 0.2µm-filtered solution in PBS.

After opening, prepare aliquots and store at -20°C.Avoid freeze/thaw cycles.For maximum product recovery after thawing, centrifuge the vial before opening the cap.

Protein. Fibrinogen-like domain of human ANGPTL4 (aa 166-406) is fused at the N-terminus to a FLAG®-tag. Source: HEK 293 cells. Endotoxin content: <0.1EU/µg purified protein (LAL test; Lonza). Liquid. 0.2µm-filtered solution in PBS. Purity: >90% (SDS-PAGE). ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.

~35kDa (SDS-PAGE)

Q9BY76

Plastic Vial

ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.

>90% (SDS-PAGE)

Fibrinogen-like domain of human ANGPTL4 (aa 166-406) is fused at the N-terminus to a FLAG®-tag.

HEK 293 cells

FLAG

Non-hazardous

Other Proteins

12352202

Stable for at least 6 months after receipt when stored at -20°C. Working aliquots are stable for up to 3 months when stored at -20°C.