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.
A synthetic peptide from human VASP
A synthesized peptide derived from human V-ATPase H, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human VAV1, corresponding to a region within N-terminal amino acids.
A synthesized peptide derived from human VAV2, corresponding to a region within N-terminal amino acids.
A synthesized peptide derived from human VBP1.
A synthesized peptide derived from human VCAM1, corresponding to a region within the internal amino acids.
VCAM-1 (CD106), a member of the immunoglobulin superfamily, is a cell surface protein expressed by activated endothelial cells and certain leukocytes (such as macrophages). VCAM-1 expression is induced by IL-1 beta, IL-4, TNF-alpha and IFN-gamma. VCAM-1 binds to leukocyte integrins VLA-4 and alpha 4 beta 7. The human and mouse VCAM-1 proteins share approximately 76% amino acid similarity.
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