Zebrafish VEGF Antibody Summary
Accession # O73682
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Cell Proliferation Induced by VEGF165and Neutralization by Zebrafish VEGF Antibody. Recombinant Zebrafish VEGF165(Catalog # 1247-ZV) stimulates proliferation in HUVEC human umbilical vein endothelial cells in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Zebrafish VEGF165(80 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Zebrafish VEGF Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1247). The ND50is typically 0.3-0.6 µg/mL.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF) and VEGF-A, is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. It is a member of the PDGF family that is characterized by the presence of eight conserved cysteine residues. In human, at least eight alternate splice isoforms of VEGF-A, ranging from 206 amino acids (aa) to 121 aa in length, are known. In zebrafish, two VEGF isoforms, a 165 aa and a 121 aa isoform, have been reported. Mature zebrafish VEGF165 shares 64%, 62% and 62% aa sequence identity with frog, human, and mouse VEGF165, respectively. There are two tyrosine kinase receptors for VEGF reported in mammals termed VEGF R1 and VEGF R2/FLK-1. One receptor has been identified in zebrafish (FLK-1), and this may actually represent the orthologue to the early common ancestor for mammalian VEGF R1 and R2. All receptors are type I transmembrane proteins that show seven immunoglobulin-like domains extracellularly and a split kinase domain intracellularly. In addition to the tyrosine kinase receptors, neuropilin-1 (NRP-1) has been reported to be a coreceptor for VEGF binding. It is proposed that the presence of NRP-1 lowers the concentration of VEGF necessary for activation of VEGF R2. NRP-1 has been reported in both zebrafish and human. VEGF regulates multiple biological functions in endothelial cells, including cell proliferation, migration and survival. These functions of VEGF are mediated partly through the induction of nitric oxide and prostacyclin, as well as up‑regulation of metalloproteinases. Together with other vascular-specific growth factors such as the Angiopoietins, VEGF have separate but complementary roles in angiogenesis and vasculogenesis (1‑7).
- Laing, D. et al. (1998) Biochem. Biophys. Acta 1397:14.
- Laing, D. and R. Ge (1998) GenBank Accession # AAC14713.
- Laio, W. et al. (1997) Development 124:381.
- Lee, P. et al. (2002) Proc. Natl. Acad. Sci. USA 99:10470.
- Thurston, G. (2002) J. Anat. 200:575.
- Zachary, I. and G. Gliki (2001) Cardiovasc. Res. 49:568.
- Robinson, C.J. and S.E. Stringer (2001) J. Cell. Sci. 114:853.
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