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Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq. DescriptionThis is a peptide mapping to a domain near the amino terminus of Human VEGF. The vascular endothelial growth factor (VEGF) family currently includes VEGF (VEGF-A), VEGF-B, VEGF-C, VEGF-D, VEGF-E, and PIGF (1). VEGF and its receptor system have been shown to be the fundamental regulators in the cell signaling of angiogenesis (2). Most tumors have the absolute requirement of angiogenesis and VEGF has been described as the most potent angiogenic cytokine linked to this process (3&4). To date 5 different isoforms of VEGF have been described, VEGF 121, VEGF 145, VEGF 165, VEGF 165b, and VEGF 189(4&5). These isoforms are generated as the result of alternative splicing from a single VEGF gene. These various isoforms have been shown to bind to two tyrosine-kinase receptors flt-1 (VEGFR-1) and flk-1/KDR (VEGFR-2), which have been found to be expressed almost exclusively on endothelial cells (5). Applications ReportedFor research use only, not for diagnostic or therapeutic use. This blocking peptide has been reported for use in competition studies. References
1. Matsumoto T, Claesson-Welsh L. 2001. VEGF receptor signal transduction. Sci STKE 112:RE21. 2. Shibuya M. 2001. Structure and function of VEGF/VEGF-receptor system involved in angiogenesis. Cell Struct Funct 26(1):25-35. 3. Hasan J, Jasyson GC. 2001. VEGF antagonists. Expert Opin Biol Ther 1(4):703-18. 4. Bates DO, Cui TG, Doughty JM, Winkler M, Sugiono M, Shields JD, Peat D, Gillatt D, Harper SJ. 2002. VEGF165b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma. Cancer Res 62(14):4123-31. 5. Neufel G, Cohen T, Gengrinovitch S, Poltorak Z. 1999. Vascular endothelial growth factor (VEGF) and its receptors. FASEB 13(1):9-22. Related ProductsCat. 14-6751 Purified anti-human VEGF polyclonal (clone Polyclonal) |
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