Application Note: VEGF-165 Recombinant Protein has been tested by SDS-PAGE and is suitable as a control for polyclonal or monoclonal anti-VEGF-165 in immunological assays.
Concentration Value: 0.1 mg/mL
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Other Performance Data: Biological Activity: Human recombinant VEGF-165 is fully biologically active when compared to standards. The ED50, as determined by the dose dependent induction of HUVEC proliferation, is 3.1-4.6 ng/ml.Endotoxin Level: Measured by LAL is <0.01ng/µg or <0.1EU/µg.
Physical State: Lyophilized
Purity and Specificity: Purity was determined to be greater than 95% as determined by analysis by RP-HPLC and by reducing and non-reducing SDS-PAGE against known standard.
Background: 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 E.coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38231 Daltons.
Low Endotoxin: Yes
Other: User Optimized