Lane 1: Hela
Lane 2: MCF-7
Lane 3: HT29
Recombinant Rabbit monoclonal primary
Recombinant VASP Monoclonal Antibody (ET1607-6)
HT29, MCF-7, Hela.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
Vasodilator stimulated phosphoprotein antibody; Vasodilator-stimulated phosphoprotein antibody; VASP antibody; VASP_HUMAN antibody
Belongs to the Ena/VASP family.
Highly expressed in platelets.
Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-157, the preferred site for PKG/PRKG1, Ser-239. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239. Phosphorylation at Ser-157 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-322 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239. Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239.
Cytoplasm, Cell junction, Cell projection.
The Wiskott-Aldrich syndrome (WAS) is characterized by thrombocytopenia, eczema, defects in cell-mediated and humoral immunity, and a propensity for lymphoproliferative diseases. The syndrome is the result of a mutation in the gene encoding a proline-rich protein termed WASP. WASP has been identified as a downstream effector of Cdc42 and has been implicated in Actin polymer-ization and cytoskeletal organization. A distantly related protein, VASP (vaso-dilator-stimulated phosphoprotein), is involved in the maintenance of cytoarchitecture by interacting with Actin-like filaments. VASP shares a limited degree of homology with the amino-terminus of WASP, which is frequently mutated in WAS patients. An established substrate of cAMP and cGMP de-pendent kinases, VASP is phosphorylated on a regulatory Serine residue 157 and localizes to focal adhesions, microfilaments and highly active regions of the plasma membrane. VASP is highly expressed in human platelets and, like WASP, may play a role in cytoskeletal organization.