Vasohibin-2, also known as VASH2, is a 355 amino acid protein belonging to the Vasohibin family. Expressed in various embryonic organs, Vasohibin-2 can be detected during embryonic weeks six through twelve and is found in vessels of 20-week embryonic organs as well as in endothelial cells of neonatal large vessels. Induced by VEGF, Vasohibin-2 is an angiogenesis inhibitor and interferes with the proliferation, migration and network formation by endothelial cells.
A synthesized peptide derived from human VASP, corresponding to a region within the internal amino acids.
A synthesized peptide derived from Human Vaspin.
Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.
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