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Background
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EGFR is a transmembrane glycoprotein that is a member of a family of protein tyrosine kinases crucial in maintaining a normal balance in cell growth and development. A prototype member of the type 1 receptor tyrosine kinases, EGFR is encoded by the cellular oncogene cerbB1. EGFR has an extracellular ligand binding domain, a single transmembrane region, and cytoplasmic domain which is composed of a tyrosine kinase domain and a carboxy terminal domain. The carboxy terminal domain contains at least four tyrosine autophosphorylation sites. Increased production or activation of EGFR has been associated with poor prognosis in a variety of tumors. EGFR overexpression is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
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Background
References
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- Aifa, S., et al., Exp. Cell Res. 302(1):108-114 (2005).
- Adams, T.E., et al., Growth Factors 22(2):89-95 (2004).
- Ichinose, J., et al., Biochem. Biophys. Res. Commun. 324(3):1143-1149 (2004).
- Kuribayashi, A., et al., Endocrinology 145(11):4976-4984 (2004).
- Kapoor, G.S., et al., Mol. Cell. Biol. 24(2):823-836 (2004).
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