VEGF (Vascular endothelial growth factor-121) Price
BACKGROUND: Vascular endothelial growth factor (VEGF) is a potent angiogenic factor, and its expression is induced by hypoxia. VEGF also
possesses a non-angiogenic role important for the cardiovascular system. For instance, it can promote differentiation of stem cells into
cardiomyocytes and endothelial cells, and boost the function of mesenchymal stem cells and endothelial progenitor cells. These activities of VEGF
are mediated in part through the AKT signaling transduction pathway. In humans, alternative splicing from the single VEGF-A gene gives rise to
multiple VEGF splice variants encoding 121, 145, 165, 189, and 206 amino acids. All isoforms contain a signal peptide sequence, but only the
VEGF121, 145, and 165 species are secreted and readily diffusible presumably due to the absence of a putative heparin-binding domain. The
recombinant human VEGF121 is expressed as a GST-fusion protein. The fusion junction of the protein harbors an engineered thrombin cleavage
site and a protein kinase A (PKA) phosphorylation site. The GST portion of the fusion protein can be cleaved off by thrombin if necessary. The
fusion protein can be radioactively labeled with 32P-r-ATP and PKA. The product is for research use only.
BACKGROUND: Vascular endothelial growth factor (VEGF) is a potent angiogenic factor, and its expression is induced by hypoxia. VEGF also
possesses a non-angiogenic role important for the cardiovascular system. For instance, it can promote differentiation of stem cells into
cardiomyocytes and endothelial cells, and boost the function of mesenchymal stem cells and endothelial progenitor cells. These activities of VEGF
are mediated in part through the AKT signaling transduction pathway. In humans, alternative splicing from the single VEGF-A gene gives rise to
multiple VEGF splice variants encoding 121, 145, 165, 189, and 206 amino acids. All isoforms contain a signal peptide sequence, but only the
VEGF121, 145, and 165 species are secreted and readily diffusible presumably due to the absence of a putative heparin-binding domain. The
recombinant human VEGF121 is expressed as a GST-fusion protein. The fusion junction of the protein harbors an engineered thrombin cleavage
site and a protein kinase A (PKA) phosphorylation site. The GST portion of the fusion protein can be cleaved off by thrombin if necessary. The
fusion protein can be radioactively labeled with 32P-r-ATP and PKA. The product is for research use only.
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Biomedical Research Service
& Clinical Application
& Clinical Application
VEGF activity is assessed by its ability to activate
AKT (phosphorylation of Ser473). The figure
shows GST-VEGF121-mediated activation of AKT
in cultured C2C12 myoblasts after VEGF
treatment. Cells were serum-starved overnight,
treated with the indicated concentrations of
GST-VEGF for 30 min, and harvested for Western
blotting analysis. The figure shows that maximum
stimulation of AKT was achieved at a GST-VEGF
concentration of ~25 ng/ml. This concentration
was also found to stimulate cell proliferation.
AKT (phosphorylation of Ser473). The figure
shows GST-VEGF121-mediated activation of AKT
in cultured C2C12 myoblasts after VEGF
treatment. Cells were serum-starved overnight,
treated with the indicated concentrations of
GST-VEGF for 30 min, and harvested for Western
blotting analysis. The figure shows that maximum
stimulation of AKT was achieved at a GST-VEGF
concentration of ~25 ng/ml. This concentration
was also found to stimulate cell proliferation.