Technical Data
V2110-04R
Vascular Endothelial Growth Factor-121, Recombinant, Human (VEGF-121)
2ug
10ug
10ug
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Technical Data |
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V2110-04R |
Vascular Endothelial Growth Factor-121, Recombinant, Human (VEGF-121) |
2ug 10ug |
| Growth Factors, Cytokines | Storage: -20°CShipping: RT |
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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-121 is a double, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28423 Dalton. VEGF-121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Ala-Glu. Dimers and Aggregates: 1% as determined by silver-stained SDS-PAGE gel analysis. 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 0.2-0.4ng/ml. Protein Content: Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm 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: Lyophilized powder may be stored at 4°C for short-term only. Reconstitute to nominal volume by adding sterile dH2O, 0.1% HSA or BSA and store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer. |
Source: E. coli. Purity: 98% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified. . 0.1ng/ug (IEU/ug). Concentration: ~0.1mg/ml Form: Supplied as a lyophilized powder. No additives. Reconstitute in ddH2O, 0.1% HSA or BSA to >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. |
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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. Vascular endothelial growth factor A (VEGF-A) is involved in guidance of VEGF receptor-positive cells to the anterior portion of early embryos. Hiratsuka S, Kataoka Y, Nakamura K, Maru Y, Mol Cell Biol 2005 Jan;25(1):355-63 3. GM-CSF induces expression of soluble VEGF receptor-1 from human monocytes and inhibits angiogenesis in mice. Eubank TD, Roberts R, Wang Y, Immunity 2004 Dec;21(6):831-42 4. ErbB2 overexpression in mammary cells upregulates VEGF through the core promoter. Loureiro RM, Maharaj AS, Muller WJ, Biochem Biophys Res Commun 2005 Jan 14;326(2):455-65 5. Localization of the VEGF and angiopoietin genes in uterine carcinosarcoma. Emoto M, Charnock-Jones DS, Ishiguro M, Hachisuga T, Gynecol Oncol 2004 Dec;95(3):474-82 6. 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.
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