Phospho-Afadin (Ser1718) Antibody #5485

In multicellular organisms, intercellular junctions play essential roles in tissue integrity and maintenance of cell polarity. Tight junctions (TJs) form a continuous barrier to fluids across the epithelium and endothelium (reviewed in 1). Adherens junctions (AJs) are dynamic structures that form cell-cell contacts linking cells into a continuous sheet (reviewed in 2). The actin filament-binding protein, Afadin, binds to nectin forming a connection to the actin cytoskeleton (3). AJs are formed when nectin assembles cadherin at the cell-cell adhesion site and these junctions are then involved in the formation and maintenance of TJs (4,5). Afadin has two splice variants: l-afadin, which is ubiquitously expressed, and s-afadin, which is expressed predominantly in neural tissue. s-Afadin is a shorter form lacking one of the three proline-rich regions found in l-afadin, as well as the carboxyl-terminal F-actin binding region (6). Human s-afadin is identical to AF-6, the ALL-1 fusion partner involved in acute myeloid leukemias (7). Recent work has also shown that afadin is involved in controlling the directionality of cell movement when it is localized at the leading edge of moving cells (8,9).
Phospho-Afadin (Ser1718) Antibody is directed at a site that was identified at Cell Signaling Technology (CST) using PhosphoScan^®, CST's LC-MS/MS platform for modification site discovery. Phosphorylation at Ser1718 was discovered using an Akt substrate antibody. Please visit PhosphoSitePlus^®, CST's modification site knowledgebase, at www.phosphosite.org for more information.