The antibody detects endogenous level of p62Dok only when phosphorylated at tyrosine 362.
Purification
The antibody 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.
Immunogen
Peptide sequence around phosphorylation site of pTyr362 (P-I-Y (p) -D-E) derived from Human p62Dok. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
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.