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Vascular Endothelial Growth Factor (VEGF)

Vascular Endothelial Growth Factor (VEGF) #9943

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# Product Name Application Reactivity

Western blot analysis of extracts from HUVE cells, untreated or VEGF165 stimulated (100 ng/ml for 5 min), using Phospho-VEGF Receptor 2 (Tyr1175) (19A10) Rabbit mAb #2478 (upper) or VEGF Receptor 2 (55B11) Rabbit mAb #2479 (lower).

Product Usage Information

CST recommends using 50-100 ng/ml of VEGF for stimulation of VEGF signaling.


Vascular Endothelial Growth Factor (VEGF) is supplied as a solution. It should be stored at –80°C. Aliquot the reagent upon receipt and avoid repeat freeze-thaw cycles.

Product Description

The human VEGF165 coding cDNA was subcloned into an expression vector and expressed in yeast. The recombinant human VEGF 165 homodimer was purified and stored in PBS buffer (pH 7.4) containing 0.1% BSA.




5x105 IU/mg

Source / Purification

Human Recombinant Protein


VEGF is a heparin-binding glycoprotein that is secreted as a homodimer of 45 kDa. Five human VEGF mRNA species encoding VEGF isoforms of 121, 145, 165, 189, and 206 amino acids are produced by alternative splicing of the VEGF mRNA from a single gene (1). Transcripts encoding VEGF165 and VEGF121 are detected in the majority of cells and tissues expressing the VEGF gene. VEGF121 lacks the amino acids encoded by exon 7 of the VEGF gene, which is present in VEGF165 and enables the ability of VEGF165 to bind to heparin and heparan sulfate. Heparin-binding VEGF165 is the best characterized VEGF species. The binding of VEGF165 to the VEGF receptors of vascular endothelial cells is modulated by the addition of exogenous heparin or heparan sulfate and inhibited after digestion of endothelial cells with heparinase (2). Neuropilin-1 is also a VEGF165 isoform specific receptor. It has been reported that neuropilin-1 can enhance the binding of VEGF165 to the Flk-1/KDR receptor (3). VEGF165 expression is regulated by various stimuli including growth factors, cytokines, gonadotropins, nitric oxide, hypoxia, hypoglycemia and oncogenic mutations.

  1. Houck, K. A. et al. (1991) Mol Endocrinol 5, 1806-1814.
  2. Gitay-Goren, H. et al. (1992) J. Biol. Chem. 267, 6093-6098.
  3. Soker, S. et al. (1998) Cell 92, 735-745.
  4. Loureiro, R.M. and D'Amore, P.A. (2005) Cytokine Growth Factor Rev. 16, 104-113.

Pathways & Proteins

Explore pathways + proteins related to this product.

For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

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