ANGPTL4 Antibody [Kairos4-397G] | 36-049

ANGPTL4 Antibody [Kairos4-397G] | 36-049 | Gentaur UK, US & Europe Distribution

Host: Mouse

Reactivity: Human

Homology: N/A

Immunogen: Recombinant human coiled-coil domain of ANGPTL4.

Research Area: Cancer, Obesity

Tested Application: E, WB

Application: ELISA: (direct or indirect: 1:500-1:5, 000) . Western blot: (1:500-1:5, 000 using ECL. Suggested blocking and dilution buffer is PBST with 0.05% Tween 20 and 5% skim milk. Suggested incubation time is 1 hour at room temperature) . Optimal conditions should be determined individually for each application.

Specificiy: Recognizes the coiled-coil domain (CCD) of human ANGPTL4. Detects a band of ~19kDa by Western blot.

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: N/A

Validation: N/A

Isoform: N/A

Purification: N/A

Clonality: Monoclonal

Clone: Kairos4-397G

Isotype: IgG1, kappa

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Liquid. 0.2um-filtered solution in PBS, pH 7.4. Contains no preservatives.

Concentration: 1 mg/ml

Storage Condition: Stable for at least 1 year after receipt when stored at -20˚C.

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

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: 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.