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Immunohistochemical staining of ANGPTL4 using anti-ANGPTL4 (coiled-coil domain) (human), mAb (Kairos4-397G) (Prod. No. AG-20A-0047) in human placenta tissue (10microg/ml). This antibody has been tested in immunohistochemistry, analyzed by an anato
Immunohistochemical staining of ANGPTL4 using anti-ANGPTL4 (coiled-coil domain) (human), mAb (Kairos4-397G) (Prod. No. AG-20A-0047) in human placenta tissue (10microg/ml). This antibody has been tested in immunohistochemistry, analyzed by an anato
Immunohistochemical staining of ANGPTL4 using anti-ANGPTL4 (coiled-coil domain) (human), mAb (Kairos4-397G) (Prod. No. AG-20A-0047) in human placenta tissue (10microg/ml). This antibody has been tested in immunohistochemistry, analyzed by an anato

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

Research Use Only
AG-20A-0047
AdipoGen Life Sciences
ApplicationsWestern Blot, ELISA, ImmunoHistoChemistry
Product group Antibodies
ReactivityHuman
TargetANGPTL4
Price on request
Packing Size
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Overview

  • Supplier
    AdipoGen Life Sciences
  • Product Name
    anti-ANGPTL4 (coiled-coil domain) (human), mAb (Kairos4-397G)
  • Delivery Days Customer
    10
  • Antibody Specificity
    Recognizes the coiled-coil domain (CCD) of human ANGPTL4. Detects a band of ~19kDa by Western blot.
  • Applications
    Western Blot, ELISA, ImmunoHistoChemistry
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    Kairos4-397G
  • Concentration
    Delete
  • Gene ID51129
  • Target name
    ANGPTL4
  • Target description
    angiopoietin like 4
  • Target synonyms
    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
  • Host
    Mouse
  • Isotype
    IgG1
  • Scientific Description
    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.
  • Reactivity
    Human
  • Storage Instruction
    2°C to 8°C,-20°C
  • UNSPSC
    12352203