VASP(Phospho Ser238) Polyclonal Antibody

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.

Introducing the VASP(PHOSPHO SER238) Polyclonal Antibody, a highly specific and reliable tool for the detection and quantification of VASP protein phosphorylated at serine 238. This antibody has been extensively validated for use in a wide range of applications, including Western blotting, immunoprecipitation, and immunofluorescence microscopy.

The VASP(PHOSPHO SER238) Polyclonal Antibody is produced using state-of-the-art techniques and high-quality materials, ensuring exceptional sensitivity and specificity. It has been rigorously tested to ensure minimal cross-reactivity with other proteins, providing accurate and reliable results every time.

This antibody is suitable for use in a variety of research areas, including cell biology, signal transduction, and cancer research. Its high specificity and sensitivity make it an ideal tool for studying the role of VASP in cellular processes such as cell migration, adhesion, and cytoskeletal organization.

In summary, the VASP(PHOSPHO SER238) Polyclonal Antibody is a top-quality research tool that offers exceptional performance and reliability. Its high specificity and sensitivity make it an essential tool for researchers studying VASP and its role in cellular processes.