anti-ANGPTL4 (coiled-coil domain) (human), mAb (Kairos4-397G)

AdipoGen Life Sciences

anti-ANGPTL4 (coiled-coil domain) (human), mAb (Kairos4-397G)

10

Western Blot, ELISA, ImmunoHistoChemistry

Research Use Only

Monoclonal

Kairos4-397G

Delete

ANGPTL4

angiopoietin like 4

angiopoietin-related protein 4; ARP4; fasting-induced adipose factor; FIAF; HARP; hepatic angiopoietin-related protein; hepatic fibrinogen/angiopoietin-related protein; HFARP; NL2; peroxisome proliferator-activated receptor (PPAR) gamma induced angiopoietin-related protein; PGAR; pp1158; PPARG angiopoietin related protein; TGQTL; UNQ171

Mouse

IgG1

Angiopoietin-related protein 4

ANGPTL4 mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorgenesis 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. - Monoclonal Antibody. Recognizes the coiled-coil domain (CCD) of human ANGPTL4. Detects a band of ~19kDa by Western blot. Isotype: Mouse IgG1kappa. Clone: Kairos4-397G. Applications: ELISA, IHC, WB. Liquid. 0.2microm-filtered solution in PBS, pH 7.4. Contains no preservatives. ANGPTL4 mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorgenesis 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.

-20°C,2°C to 8°C

12352203