VEGF-A (mouse) ELISA

One of the key molecules for angiogenesis and for the survival of the endothelium is vascular endothelial growth factor (VEGF-A). It is a specific endothelial cell mitogen and a strong vascular permeability factor (VPF). VEGF-A is a heparin-binding glycoprotein, secreted as a homodimer of 45 kDa by many different cell types. VEGF-A also causes vasodilation through the nitiric oxide synthase pathway in endothelial cells and can activate migration in monocytes. Many different splice variants of VEGF-A have been described, but VEGF165 is the most predominant protein and anchors with its heparin binding domain to extracellular matrix and to heparin sulfate. Examples where VEGF-A plays an important role are psoriasis andrheumatoid arthritis, as well as the ovarian hyperstimulation syndrome. Diabetic retinopathy is associated with high intraocular levels of VEGF-A, and inhibition of VEGF-A function may result in infertility by blockage of corpus luteum function. Direct demonstration of the importance of VEGF-A in tumor growth has been achieved using dominant negative VEGF receptors to block in vivo proliferation, as well as blocking antibodies to VEGF or to one of the VEGF receptors. VEGF-A transcription is highly activated by hypoxia and by oncogenes like H-ras and several transmembrane tyrosine kinases, such as epidermal growth factor receptor and ErbB2. Together these pathways account for a marked upregulation of VEGF-A in tumors compared to normal tissues and are often of prognostic importance and relevance. Targeting the VEGF signalling may be of major therapeutic importance for many diseases and serves as a basis for the design of future (anti)-angiogenic treatments. Synonyms: Vascular endothelial growth factor A, VPF