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.1) Barragan, P., et al. Thromb. Haemost. 104(2):410-411(2010) More
This VASP antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 267-296 amino acids from the C-terminal region of human VASP.
IHC-PWB
Human
Western Blot at 1:2000 dilution Lane 1: A549 whole cell lysate Lane 2: Hela whole cell lysate Lane 3: HepG2 whole cell lysate Lane 4: HUVEC whole cell lysate Lane 5: MDA-MB-453 whole cell lysate Lane 6: THP-1 whole cell lysate Lysates/proteins at 20 ug per lane.
VASP Antibody immunohistochemistry analysis in formalin fixed and paraffin embedded human tonsil tissue followed by peroxidase conjugation of the secondary antibody and DAB staining.
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