Technical Data
V2110-04A
Vascular Endothelial Growth Factor, Recombinant, Human (VEGF)
2ug
10ug
Growth Factors, Cytokines Storage: -20CShipping: RT
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 is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38231 Dalton.

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

Biological Activity:
The biological activity is determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 1.0-8.0ng/ml.

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 calibrated solution of VEGF as a Reference Standard.

Storage and Stability:
Store at -20C. Reconstitute to nominal volume by adding sterile dH2O, 0.1% HSA or BSA and store at -20C. Reconstituted product is stable for 12 months at -20C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.
Source: Recombinant, Human (Escherichia coli)
Purity: >98% by RP-HPLC and reducing/non-reducing SDS-PAGE (silver stained)
Concentration: ~0.1mg/ml
Form: Supplied as a lyophilized powder. No additives. Reconstitute with sterile ddH2O, 0.1% HSA or BSA to a concentration 0.1mg/ml

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.
1. Overproduction of VEGF concomitantly expressed with its receptors promotes growth and survival of melanoma cells through MAPK and PI3K signaling. Graells J, Vinyals A, Llorens A, Fabra A, J Invest Dermatol 2004 Dec;123(6):1151-61 2. Differential effects of antiangiogenic compounds in neovascularization, leukocyte recruitment, VEGF production, and tumor growth in mice. Belo AV, Barcelos LS, Ferreira MA, Cancer Invest 2004;22(5):723-9 3. Molecular regulation of the VEGF family -- inducers of angiogenesis and lymphangiogenesis. McColl BK, Stacker SA, APMIS 2004 Jul-Aug;112(7-8):463-80 4. Characterization of vascular endothelial growth factor (VEGF) in the uterine cervix over pregnancy: effects of denervation and implications for cervical ripening. Mowa CN, Jesmin S, Usip S, Papka R, J Histochem Cytochem 2004 Dec;52(12):1665-74 5. VEGF concentrations in pregnancy. Bussen S, Dietl J, Am J Obstet Gynecol 2004 Nov;191(5):1834 6. The involvement of growth hormone (GH), insulin-like growth factors (IGFs) and vascular endothelial growth factor (VEGF) in diabetic kidney disease. Flyvbjerg A, Khatir DS, Dagnaes-Hansen F, Curr Pharm Des 2004;10(27):3385-94.

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