The epidermal growth factor receptor (EGFR) is over-expressed in various human epithelial tumors usually due to the gene amplification. EGFR gene amplification in tumors frequently contain its rearrangements and among them, the most common extracellular domain mutation is receptor variant III, EGFRvIII (also known as de2-7EGFR or DEGFR). The molecular mass of EGFRvIII is approximately 145 kDa and this genetic change of tumor-specific mutation results from a deletion of 267 amino acids spanning exons 2-7 of the EGFR gene. These consequences make the variant EGFRvIII incapable of binding known ligand. It is expressed in a majority of patients with glioblastoma multiforme. And the evidence shows aberrant EGFRvIII signaling is important for driving tumor progression. HER2 (Human epidermal growth factor receptor 2), also known as ERBB2, CD340 (cluster of differentiation 340), proto-oncogene Neu, is a membrane tyrosine kinase and has strongest catalytic kinase activity in HER family. Among four HER family proteins, HER2 functions as the most active signaling complex after dimerization with other members. It is encoded by the oncogene ERBB2, which is located at the human chromosome 17q12. HER2 participates in normal cell growth and found on some types of cancer cells. Its amplification is the major pathway causing HER2 receptor overexpression. HER2 is amplified in approximately 15%-20% of breast cancers and functions as the primary driver in breast tumor development and progression. The overexpressed HER2 is regarded as a valuable target in clinic therapeutics.