The IGF-I receptor (IGF-IR) plays an important role in cell growth control, in malignant transformation, and in cell survival. Its role in human cancer has been firmerly established. High level of IGF-IR in breast cancer is highly correlated with ipsilateral breast tumor recurrence following lumpectomy and radiation therapy. IGF-IR signaling occurs upon activation by its ligands, that induce autophosphorylation of the receptor at several tyrosine residues.. Phosphorylation of tyrosine residue at position 1316 (Y1316) is necessary for tumor formation in nude mice, although not essential for IGF-I-induced mitogenesis. We generated a rabbit polyclonal antibody that specifically recognizes a phosphorylated IGF-IR. This antibody (anti-pY1316/IGF-IR) do not crossreact with a phosphorylated Insulin receptor, and do not recognizes a C-terminus-truncated IGF-IR nor a mutant IGF-IR having the Y1316 replaced with phenylalanine (Y1316F). The anti-pY1316/IGF-IR antibody can be used in immunohistchemistry and can be applied for the detection of activated IGF-IRs in human tumor sections. Analyses of Y1316-IGF-IR phosphorylation level are in progress to establish whether this parameter may have a prognostic value in human breast cancer.
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