ANGPTL4 (mouse) (rec.)
Product Code:
AG-40A-0075
AG-40A-0075
Host Type:
Monkey
Monkey
Regulatory Status:
RUO
RUO
Target Species:
Mouse
Mouse
Shipping:
Blue Ice
Blue Ice
Storage:
-20°C
-20°C
No additional charges, what you see is what you pay! *
Code | Size | Price |
---|
AG-40A-0075-C010 | 10 ug | £150.00 |
Quantity:
AG-40A-0075-C050 | 50 ug | £290.00 |
Quantity:
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This product comes from: Switzerland.
Typical lead time: 7-10 working days.
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Typical lead time: 7-10 working days.
Contact us for more accurate information.
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Further Information
Alternate Names/Synonyms:
Angiopoietin-like Protein 4; FIAF; Fasting-induced Adipose Factor; HFARP; Hepatic Fibrinogen/Angiopoietin-related Protein
Biological Activity:
Activates ERK phosphorylation in THP-1 cells.
Concentration:
0.5mg/ml
EClass:
32160000
Endotoxin:
<0.1EU/µg purified protein (LAL test; Lonza).
Form (Short):
liquid
Formulation:
Liquid. 0.2µm-filtered solution in PBS.
Handling Advice:
After opening, prepare aliquots and store at -20°C.Avoid freeze/thaw cycles.For maximum product recovery after thawing, centrifuge the vial before opening the cap.
Long Description:
Protein. Mouse ANGPTL4 (aa 1-410) is fused at the C-terminus to a FLAG®-tag. Source: COS-7 cells. Endotoxin content: <0.1EU/µg purified protein (LAL test; Lonza). Liquid. 0.2µm-filtered solution in PBS. Purity: >90% (SDS-PAGE). 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:
~50kDa (SDS-PAGE)
NCBI, Uniprot Number:
Q9Z1P8
Package Type:
Plastic Vial
Product Description:
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.
Purity:
>90% (SDS-PAGE)
Sequence:
Mouse ANGPTL4 (aa 1-410) is fused at the C-terminus to a FLAG®-tag.
Source / Host:
COS-7 cells
TAGs:
FLAG
Transportation:
Non-hazardous
UNSPSC Category:
Other Proteins
UNSPSC Number:
12352202
Use & Stability:
Stable for at least 6 months after receipt when stored at -20°C. Working aliquots are stable for up to 3 months when stored at -20°C.
Documents
References
Regulation of energy balance by the hypothalamic lipoprotein lipase regulator Angptl3: H.K. Kim, et al.; Diabetes 64, 1142 (2015)
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