Phospho-ALK (Tyr1507) (D6F1V) Rabbit Monoclonal Antibody recognizes endogenous levels of ALK protein only when phosphorylated at Tyr1507 (equivalent to Tyr567 of NPM-ALK).

Mouse, Rat

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1507 of human ALK protein.

Anaplastic lymphoma kinase (ALK) is a tyrosine kinase receptor for pleiotrophin (PTN), a growth factor involved in embryonic brain development (1-3). In ALK-expressing cells, PTN induces phosphorylation of both ALK and the downstream effectors IRS-1, Shc, PLCγ, and PI3 kinase (1). ALK was originally discovered as a nucleophosmin (NPM)-ALK fusion protein produced by a translocation (4). Investigators have found that the NPM-ALK fusion protein is a constitutively active, oncogenic tyrosine kinase associated with anaplastic lymphoma (4). Research literature suggests that activation of PLCγ by NPM-ALK may be a crucial step for its mitogenic activity and involved in the pathogenesis of anaplastic lymphomas (5).
A distinct ALK oncogenic fusion protein involving ALK and echinoderm microtubule-associated protein like 4 (EML4) has been described in the research literature from a non-small cell lung cancer (NSCLC) cell line, with corresponding fusion transcripts present in some cases of lung adenocarcinoma. The short, amino-terminal region of the microtubule-associated protein EML4 is fused to the kinase domain of ALK (6-8).
Phosphorylation of ALK on Tyr1507 was identified at Cell Signaling Technology using PhosphoScan^®, an LC-MS/MS platform used for phosphorylation site discovery (6). Phosphorylation of ALK at Tyr1507 (Tyr567 in NPM-ALK) has been shown to be important for interaction with the adaptor proteins Shc, FRS2-α, and FRS2-β (9,10).