The insulin receptor (IR) is an ancient tyrosine kinase (TK) receptor found across a wide phylogeny of organisms, ranging from those as primitive as cnidarians and insects through to vertebrates. In higher organisms, it plays an essential role in glucose homeostasis[1]. In mammals, the insulin receptor (IR) gene has acquired an additional exon, exon 11. This exon may be skipped in a developmental and tissue-specific manner. The IR, therefore, occurs in two isoforms (exon 11 minus IR-A and exon 11 plus IR-B). IR-A is predominantly expressed during prenatal life. It enhances the effects of IGF-II during embryogenesis and fetal development. It is also significantly expressed in adult tissues, especially in the brain. Conversely, IR-B is predominantly expressed in adult, well-differentiated tissues, including the liver, where it enhances the metabolic effects of insulin. Dysregulation of IR splicing in insulin target tissues may occur in patients with insulin resistance; however, its role in type 2 diabetes is unclear. The recognition that IR-A is aberrantly expressed in cancer cells has provided a framework for better understanding of the cancer-promoting effects of hyperinsulinemia. Moreover, both insulin and IGFs synergize with sex steroids in the promotion of sex steroid-sensitive tumors. Taken together, inhibition of IR underscore the utility of preventing the development of obesity and T2DM and consequent hyperinsulinemia as an effective cancer prevention strategy[2].