Technical Data
Vascular Endothelial Growth Factor, Recombinant, Human (VEGF, MGC70609, Vascular Endothelial Growth Factor A precursor, Vascular Permeability Factor, VEGFA, VEGF-A, VPF)
Molecular Biology Storage: -20CShipping: Blue Ice
Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as Tumor Angiogenesis Factor or Vascular Permeability Factor. Although expressed at high levels in certain tumor-derived cells it is produced by a wide variety of cell types. In addition to stimulating vascular growth and vascular permeability it may play a role in stimulating Vasolidation via nitric oxide-dependent pathways. Alternative splicing of the mRNA for VEGF-A results in several isoforms of the protein being produced. Rat and bovine VEGF are one amino acid shorter than the human factor, and the bovine and human sequences show a homology of 95 percent. In contrast to other factors mitogenic for endothelial cells such as FGF-1, FGF-2 and PDGF, VEGF is synthesized as a precursor containing a typical hydrophobic secretory signal sequence of 26 amino acids. Glycosylation is not required for efficient secretion of VEGF.

Recombinant Human VEGF produced in HEK293 cells is a double, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 40kD.

Amino Acid Sequence:

Biological Activity:
Recombinant VEGF is fully biologically active when compared to standards. Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 1-6ng/ml, corresponding to a specific activity of 1x10e6 Units/mg to 1.7x10e5Units/mg.

Protein Content:
Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280nm using the absorbency value of 0.2875 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
2. Analysis by RP-HPLC, using a standard solution of BDNF as a Reference Standard.

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 12 months after receipt at -20C. Reconstitute with sterile ddH2O, 0.1% HSA or BSA. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Molecular Weight:
Source: HEK293 (Human Embryonic Kidney Cell Line
Purity: ~95% by SDS-PAGE
Form: Supplied as a lyophilized powder without additives. Reconstitute with sterile ddH2O, 0.1% HSA or BSA to a concentration of 100ug/ml, which can then be further diluted to other aqueous solutions.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
US Biological application reference: Morohoshi, K. et al., (2011) Experimental and Molecular Pathology, doi:10.1016/j.yexmp.2011.09.017. 1. Vascular-endothelial-growth-factor (VEGF) expression and possible response to angiogenesis inhibitor bevacizumab in metastatic alveolar soft part sarcoma. Lancet Oncol 2006 Jun;7(6):521-3 2. VEGF165b, an endogenous C-terminal splice variant of VEGF, inhibits retinal neovascularization in mice. Mol Vis 2006 May 26;12:626-32 3. Angiostatin decreases cell migration and vascular endothelium growth factor (VEGF) to pigment epithelium derived factor (PEDF) RNA ratio in vitro and in a murine ocular melanoma model. Mol Vis 2006 May 22;12:511-7 4. Signaling from across the way: transactivation of VEGF receptors by HSPGs. Mol Cell 2006 May 19;22(4):431-2 5. Phosphorylated Akt1 in human breast cancer measured by direct sandwich enzyme-linked immunosorbent assay: Correlation with clinicopathological features and tumor VEGF-signaling system component levels. Int J Biol Markers 2006 Jan-Mar;21(1):12-9 6. Study of microvessel density and the expression of the angiogenic factors VEGF, bFGF and the receptors Flt-1 and FLK-1 in benign, premalignant and malignant prostate tissues. Histol Histopathol 2006 Aug;21(8):857-65

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.