Specifications
- HOST SPECIES: Rabbit
- SPECIES REACTIVITY: Human
- IMMUNOGEN: Synthetic peptide corresponding to aa 79-101 (A79CQGTEGSTDLPLAPESRVDPEV101) of human ANGPTL4.
- CONJUGATE: Unconjugated
- TESTED APPLICATIONS: ELISA, WB
- APPLICATION NOTE: ELISA: (direct and indirect: 1:2,000-1:5,000). Western Blot: (1:2,000-1:5,000 using ECL; suggested blocking and dilution buffer is PBST containing 0.05% Tween 20 and 5% skim milk; suggested incubation time is 1 hour at room temperature). Optimal conditions must be determined individually for each application.
- SPECIFICITY: Recognizes the coiled-coil domain of human ANGPTL4. Detects a band of ~18kDa by Western blot. Weakly cross-reacts with human ANGPTL6. Does not cross-react with other ANGPTL family proteins.
Properties
- CLONALITY: Polyclonal
- PHYSICAL STATE: Liquid
- BUFFER: Liquid. 0.2um-filtered solution in PBS, pH 7.4. Contains no preservatives.
- CONCENTRATION: 1 mg/ml
- STORAGE CONDITIONS: Stable for at least 6 months after receipt when stored at -20°C.
Additional Info
- NCBI OFFICIAL SYMBOL: ANGPTL4
- ADDITIONAL NAMES: Angiopoietin-like Protein 4; FIAF; Fasting-induced Adipose Factor; HFARP; Hepatic Fibrinogen/Angiopoietin-related Protein
- Protein Accession Number: 25008123
- PROTEIN GI NUMBER: Q9BY76
- NCBI GENE ID NUMBER: 51129
- 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.
Disclaimer
- FOR RESEARCH USE ONLY
For additional information, visit ProSci's Terms & Conditions Page. - Disclaimer: Optimal dilutions/concentrations should be determined by the end user. The information provided is a guideline for product use. This product is for research use only.
Shipping Info
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