Anti-DOK1 (phospho Y398) Antibody

Docking protein 1 (DOK1) is recruited as a negative regulator of receptor tyrosine kinase and immunoreceptor signaling, and the rabbit polyclonal IgG reagent from Antibodies.com is raised specifically against the Y398 phospho-tyrosine epitope of human DOK1. Supplied as 50 µl of unconjugated antibody, the reagent is validated for Western blot (WB) and immunohistochemistry (IHC) workflows and has been confirmed to cross-react with mouse and rat orthologs in addition to human samples.

DOK1, also known as p62^dok, sits at a node where signals from receptors such as the insulin receptor, Eph receptors, and T- and B-cell antigen receptors converge on the Ras/MAPK cascade. Phosphorylation at Y398 marks the active, signaling-engaged pool of the protein and is commonly probed in studies of Ras/MAPK modulation, leukocyte activation, and receptor down-regulation. A phospho-site-specific reagent therefore lets researchers distinguish the activated state from total DOK1 levels in lysates or fixed tissue sections.

Because the antibody is delivered unconjugated as a polyclonal IgG in 50 µl, it is compatible with standard HRP- or fluorophore-conjugated secondary detection chemistries and slots into most existing WB and IHC protocols. Storage at -20 °C in small aliquots preserves phospho-epitope recognition across repeated freeze-thaw cycles for long-term use, and the polyclonal background provides a robust signal when paired with affinity-purified secondary antibodies.