Phospho-p90Rsk/RSK1/RPS6KA1-S363 Rabbit pAb

WB,1:500 - 1:1000 | IP,1:50 - 1:100

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.

Unconjugated

PBS with 0.01% thimerosal, 50% glycerol

A synthetic phosphorylated peptide around S363 of human p90Rsk/RSK1/RPS6KA1 (NP_002944.2).

83kDa

KDSPG