Human Vascular Edothelial Growth Factor (VEGF) 121-GST Protein
This recombinant human VEGF121 is expressed as a GST-fusion protein, which allows for easy detection via western blot. 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.
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.
From the laboratory of Te-Chung Lee, PhD, University at Buffalo.
Part of The Investigator's Annexe program.
This recombinant human VEGF121 is expressed as a GST-fusion protein, which allows for easy detection via western blot. 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.
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.
From the laboratory of Te-Chung Lee, PhD, University at Buffalo.
Part of The Investigator's Annexe program.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Protein |
| Name: | Vascular Endothelial Growth Factor (VEGF) 121-GST |
| Accession ID: | AF214570.1 |
| Source: | Recombinant, purified from E. coliBL21 |
| Molecular Weight: | ~40 kDa |
| Amino Acid Sequence: | MAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKCDKPRR |
| Fusion Tag(s): | GST |
| Purity: | 99% |
| Buffer: | PBS |
| Concentration: | 0.1mg/mL |
| Storage: | Store at -80C |
| Shipped: | Dry ice |
VEGF121 Activity Analysis
VEGF activity as 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.
If you publish research with this product, please let us know so we can cite your paper.
