Anti-VASP Antibody [SY02-16]

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.