ANGPTL4 antibody (AA 79-101)

Catalog No. ABIN1169314

This Rabbit Polyclonal antibody specifically detects ANGPTL4 in WB and ELISA. It exhibits reactivity toward Human.

Quick Overview for ANGPTL4 antibody (AA 79-101) (ABIN1169314)

Target: ANGPTL4 (Angiopoietin-Like 4 (ANGPTL4))

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This ANGPTL4 antibody is un-conjugated

Application: Western Blotting (WB), ELISA

Product Details anti-ANGPTL4 Antibody

Binding Specificity: AA 79-101

Specificity: Recognizes the coiled-coil domain of human ANGPTL4. Detects a band of ~18 kDa by Western blot.

Cross-Reactivity: Human

Cross-Reactivity (Details): Weakly cross-reacts with human ANGPTL6. Does not cross-react with other ANGPTL family proteins.

Sterility: 0.2 μm filtered

Immunogen: Synthetic peptide corresponding to aa 79-101 (A79CQGTEGSTDLPLAPESRVDPEV101) of human ANGPTL4.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: Lot specific

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

Preservative: Without preservative

Storage: 4 °C,-20 °C

Storage Comment: Short Term Storage: +4°C
Long Term Storage: -20°C
Stable for at least 6 months after receipt when stored at -20°C.

Expiry Date: 6 months

Target Details for ANGPTL4

Target: ANGPTL4 (Angiopoietin-Like 4 (ANGPTL4))

Alternative Name: ANGPTL4

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.

UniProt: Q9BY76

Pathways: Regulation of Lipid Metabolism by PPARalpha