Vascular Endothelial Growth Factor, Recombinant, Human (VEGF, MGC70609, Vascular Endothelial Growth Factor A precursor, Vascular Permeability Factor, VEGFA, VEGF-A, VPF)

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.\n\nRecombinant Human VEGF produced in HEK293 cells is a double, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 40kD.\n\nAmino Acid Sequence:\nAPMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR\n\nBiological Activity: \nRecombinant 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.\n\nProtein Content: \nProtein quantitation was carried out by two independent methods: \n1. 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). \n2. Analysis by RP-HPLC, using a standard solution of BDNF as a Reference Standard.\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile ddH2O, 0.1% HSA or BSA. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. 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.

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SPECIFICATIONS

Catalog Number

V2110-15D

Size

2ug

Form

Supplied as a lyophilized powder without additives. Reconstitute with sterile ddH2O, 0.1% HSA or BSA to a concentration of (same/more than)100ug/ml, which can then be further diluted to other aqueous solutions.

Purity

~95% by SDS-PAGE

References

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