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The IGF1 receptor prefers IGF1 over IGF2 and weakly binds insulin. IGF1 receptor is a disulfide-linked heterotetrameric transmembrane protein consisting of two alpha (130 kD) and two beta (95 kD) subunits. Both the alpha and beta subunits are encoded within a single receptor precursor cDNA. The IGF1 receptor is therefore similar in structure to the insulin receptor. The proreceptor polypeptide is proteolytically cleaved and disulfide-linked to yield the mature heterotetrameric receptor. The IGF1 receptor is highly expressed in all cell types and tissues and is highly overexpressed in most malignant tissues where it functions as an anti-apoptotic agent by enhancing cell survival