Anti-VEGF/Vegfa Picoband® Antibody Fluoro647 Conjugated

Vascular endothelial growth factor A (VEGF-A) is a protein that in humans is encoded by the VEGFA gene. It is mapped to 17 C; 17 22.79 cM. This gene is a member of the PDGF/VEGF growth factor family. It encodes a heparin-binding protein, which exists as a disulfide-linked homodimer. This growth factor induces proliferation and migration of vascular endothelial cells, and is essential for both physiological and pathological angiogenesis. Disruption of this gene in mice resulted in abnormal embryonic blood vessel formation. This gene is upregulated in many known tumors and its expression is correlated with tumor stage and progression. Elevated levels of this protein are found in patients with POEMS syndrome, also known as Crow-Fukase syndrome. Allelic variants of this gene have been associated with microvascular complications of diabetes 1 (MVCD1) and atherosclerosis. Alternatively spliced transcript variants encoding different isoforms have been described. There is also evidence for alternative translation initiation from upstream non-AUG (CUG) codons resulting in additional isoforms. A recent study showed that a C-terminally extended isoform is produced by use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism, and that this isoform is antiangiogenic. Expression of some isoforms derived from the AUG start codon is regulated by a small upstream open reading frame, which is located within an internal ribosome entry site.

Angiogenesis, Cancer, Cancer Metabolism, Cardiovascular, Growth Factors, Growth Factors/Hormones, Metabolism, Metabolism Processes, Pathways and Processes, Response To Hypoxia, Signal Transduction

Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. May play a role in increasing vascular permeability during lactation, when increased transport of molecules from the blood is required for efficient milk protein synthesis. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development.

1. Rao, S., Chun, C., Fan, J., Kofron, J. M., Yang, M. B., Hegde, R. S., Ferrara, N., Copenhagen, D. R., Lang, R. A. A and melanopsin-dependent fetal light response regulates mouse eye development. Nature 494: 243-246, 2013. 2. Ray, P. S., Jia, J., Yao, P., Majumder, M., Hatzoglou, M., Fox, P. L. A stress-responsive RNA switch regulates VEGFA expression. Nature 457: 915-919, 2009. 3. Ruhrberg, C., Gerhardt, H., Golding, M., Watson, R., Ioannidou, S., Fujisawa, H., Betscholtz, C., Shima, D. T. Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis. Genes Dev. 16: 2684-2698, 2002.