ANGPTL4 Protein (AA 166-406, Fibrinogen-like Domain) (DYKDDDDK Tag)
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- Target See all ANGPTL4 Proteins
- ANGPTL4 (Angiopoietin-Like 4 (ANGPTL4))
- Protein Type
- Recombinant
- Protein Characteristics
- Fibrinogen-like Domain, AA 166-406
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This ANGPTL4 protein is labelled with DYKDDDDK Tag.
- Application
- SDS-PAGE (SDS)
- Cross-Reactivity
- Human
- Characteristics
- Fibrinogen-like domain of human ANGPTL4 (aa 166-406) is fused at the N-terminus to a FLAG®-tag.
- Purity
- >90 % (SDS-PAGE)
- Sterility
- 0.2 μm filtered
- Endotoxin Level
- <0.1EU/μg purified protein (LAL test, Lonza).
- Top Product
- Discover our top product ANGPTL4 Protein
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- Lot specific
- Buffer
- 0.2μm-filtered solution in PBS.
- Storage
- 4 °C,-20 °C
- Storage Comment
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Short Term Storage: +4°C
Long Term Storage: -20°C
Working aliquots are stable for up to 3 months when stored at -20°C. - Expiry Date
- 3 months
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- Target
- ANGPTL4 (Angiopoietin-Like 4 (ANGPTL4))
- Alternative Name
- ANGPTL4 (ANGPTL4 Products)
- Synonyms
- ANGPTL2 Protein, ARP4 Protein, FIAF Protein, HFARP Protein, NL2 Protein, PGAR Protein, pp1158 Protein, Arp4 Protein, Bk89 Protein, Fiaf Protein, Hfarp Protein, Ng27 Protein, Pgar Protein, Pgarg Protein, Pp1158 Protein, ANGPTL4 Protein, fiaf Protein, im:7144703 Protein, si:rp71-39b20.7 Protein, angiopoietin like 4 Protein, angiopoietin-like 4 Protein, ANGPTL4 Protein, Angptl4 Protein, angptl4 Protein
- Background
- ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis 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.
- Molecular Weight
- ~35kDa (SDS-PAGE)
- UniProt
- Q9BY76
- Pathways
- Regulation of Lipid Metabolism by PPARalpha
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