Vascular Endothelial Growth Factor variant

human, recombinant, E. coli

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PR-690 10 μg 253,00 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped at ambient temperature

Storage Conditions: store at -20 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Molecular Weight: 28.4 kDa

Accession number: P15692

Accession number: P15692

Purity: > 95 % (SDS-PAGE, RP-HPLC)

Form: lyophilized

Solubility: It is recommended to reconstitute the lyophilized VEGF in sterile bidest H2O not less than 100 μg/ml containing at least 0.1% human serum albumin or bovine serum albumin.

Activity: ED50: 0.2 - 0.4 ng/ml, determined by the dosedependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC).

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 tumorderived 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-121 produced in E. coli is a double, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28.4 kDa. VEGF-121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant VEGF is purified by proprietary techniques.

Amino Acid Sequence: The sequence of the first five N-terminal amino acids was found to be Ala-Pro-Met-Ala-Glu.

Selected References:
Sakai et al. (2005) Plasma VEGF as a marker for the diagnosis and treatment of vasculitic neuropathy. J. Neurol. Neurosurg. Psychiatry. 76:296.
Graells et al. (2004) Overproduction of VEGF concomitantly expressed with its receptors promotes growth and survival of melanoma cells through MAPK and PI3K signaling. J. Invest. Dermatol. 123:1151.
Hiratsuka et al. (2005) Vascular endothelial growth factor A (VEGFA) is involved in guidance of VEGF receptor-positive cells to the anterior portion of early embryos. Mol. Cell. Biol. 25:355.
Nascimento et al. (2004) Vascular endothelial growth factor (VEGF) levels as a tool to discriminate between malignant and nonmalignant ascites. APMIS. 112:585.
Cisowski et al. (2005) Role of heme oxygenase-1 in hydrogen peroxide-induced VEGF synthesis: effect of HO-1 knockout. Biochem. Biophys. Res. Commun. 326:670.
Eubank et al. (2004) GM-CSF induces expression of soluble VEGF receptor-1 from human monocytes and inhibits angiogenesis in mice. Immunity. 21:831.