ab75742 was affinity purified from rabbit antiserum by affinity chromatography using epitope specific phosphopeptide. The antibody against non phosphopeptide was removed by chromatography using non phosphopeptide corresponding to the phosphorylation site.
DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3.
Expressed in pancreas, heart, leukocyte and spleen. Expressed in both resting and activated peripheral blood T-cells.
Belongs to the DOK family. Type A subfamily. Contains 1 IRS-type PTB domain. Contains 1 PH domain.
The PTB domain mediates receptor interaction.
Constitutively tyrosine-phosphorylated. Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway.
ab75742, at a 1/50 dilution, staining DOK1 in paraffin embedded human breast carcinoma tissue by Immunohistochemistry in the absence (left image) or presence (right image) of the immunizing phospho peptide.
Western blot - DOK1 (phospho Y362) antibody (ab75742)
All lanes : Anti-DOK1 (phospho Y362) antibody (ab75742) at 1/500 dilution
Lane 1 : Jurkat cell extracts with immunising peptide Lane 2 : Jurkat cell extracts
Predicted band size: 52 kDa Observed band size: 52 kDa