VEGF (vascular endothelial growth factor) is a homodimeric, disulfide-linked glycoprotein growth factor that plays a critical role in angiogenesis, vasculogenesis and endothelial cell growth through induction of endothelial cell proliferation and blood vessels permeabilization, cell migration promotion as well as inhibition of apoptosis. VEGF can bind to FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. Its isoforms VEGF189, VEGF165 and VEGF121 are widely expressed, whereas, other isoforms VEGF206 and VEGF145 are not very common. The basic isoform VEGF189 is cell-associated after secretion and is bound avidly by heparin and the extracellular matrix, although it may be released as a soluble form by heparin, heparinase or plasmin. VEGF bind to three tyrosine-kinase receptors, VEGFR-1, VEGFR-2 and VEGFR-3 which are expressed almost exclusively in endothelial cells. VEGFR-2 is the main angiogenic signal transducer for VEGF, while VEGFR-3 is specific for VEGF-C/-D (may gain VEGFR-2 binding ability via proteolytic processing) and is essential for lymphangiogenic signaling. VEGF is regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoxia, hypoglycemia and oncogenic mutations. Defects in VEGFA are linked to MVCD1 (microvascular complications of diabetes type 1) and VEGF polymorphisms are associated with susceptibility to multiple cancers, e.g., glioma, HCC, ovarian, bladder, prostate, breast cancer etc.