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Background: HER2 (ErbB2, epidermal growth factor receptor 2) is one of the four members of the ErbB receptor family of transmembrane receptor-like tyrosine kinases (1). The kinase activity of HER2 can be activated without ligand if it is overexpressed, and by association with other HER proteins (2). Overexpression of HER2 is detected in almost 40% of human breast cancers (3). Therefore, HER2 is considered one of the major targets for the treatment of breast cancer and other carcinomas. Binding of c-Cbl ubiquitin ligase to Tyr1112 of HER2 leads to poly-ubiquitination of HER2 and enhances its degradation (4). Similar to other growth factors, HER2 exhibits intrinsic protein tyrosine kinase activity and undergoes autophosphorylation (Y1023, Y1248, Y1139, and Y1222). A phosphorylation at tyrosine 1139 has been identified to induce the binding of Src to HER2, leading to HER2 activation of Stat3 alpha (5).