ANGPTL4 antibody

Catalog No. ABIN1169313

Cited in 1 publication. The Rabbit Polyclonal anti-ANGPTL4 antibody (ABIN1169313) specifically detects ANGPTL4 in WB and ELISA. The antibody is reactive with Human samples.

Quick Overview for ANGPTL4 antibody (ABIN1169313)

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

Specificity: Recognizes human ANGPTL4. Detects a band of ~35 kDa and 62 kDa by Western blot.

Cross-Reactivity: Human

Sterility: 0.2 μm filtered

Immunogen: Recombinant 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

References for anti-ANGPTL4 antibody (ABIN1169313)

Broxmeyer, Srour, Cooper, Wallace, Hangoc, Youn: "Angiopoietin-like-2 and -3 act through their coiled-coil domains to enhance survival and replating capacity of human cord blood hematopoietic progenitors." in: Blood cells, molecules & diseases, Vol. 48, Issue 1, pp. 25-9, (2012) (PubMed).

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