purified, synthetic phosphopeptide corresponding to residues surrounding tyrosine 845 of human epidermal growth factor receptor.
Biochem/physiol Actions
EGFR is a transmembrane glycoprotein that binds to the EGF family. It is a pivotal regulator of cell proliferation, growth, differentiation and DNA repair after radiation-induced damage. Mutations in the gene encoding EGFR are associated with a number of malignancies including lung cancer and colorectal cancer. Phosphorylation of Tyr845 is associated with EGFR mutation and serves as a surrogate marker.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline with 5% trehalose.
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Lung cancer (Amsterdam, Netherlands), 63(2), 241-246 (2008-07-01)
Overexpression of EGFR is found in several malignancies including lung cancers. Recently, EGFR mutation has been shown to correlate with responsiveness to tyrosine kinase inhibitors (TKI). Although antibodies against phophorylated EGFR have been used in vitro, phosphorylated EGFR has yet
Epidermal growth factor receptor (EGFR) exemplifies the family of receptor tyrosine kinases that mediate numerous cellular processes, including growth, proliferation, and differentiation. Moreover, gene amplification and EGFR mutations have been identified in a number of human malignancies, making this receptor
Asian Pacific journal of cancer prevention : APJCP, 13(10), 4879-4881 (2012-12-19)
Epidermal growth factor receptor (EGFR) overexpression is associated with resistance to chemotherapy and radiotherapy. The EGFR modulates DNA repair after radiation-induced damage through an association with the catalytic subunit of DNA protein kinase. DNA double-strand breaks (DSBs) are the most
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