EGFR

Contents: EGFR (I12) Blocking Peptide
Catalog Number: 66-P747
Formulation: Phosphate buffered saline, pH 7.2 BSA and 0.09% NaN₃
Storage Conditions: Store at 4°C.
DO NOT FREEZE.

Prices for This Product*
Cat. No.	Size	Price	Qty	Action
66-P747-81	50 ug	$25

*International customers: Please contact your distributor for region specific pricing.

Available Formats of This Product
Cat. No.	Format	Excite (nm)	Emit (nm)	Reported Applications
66-P747	Blocking Peptides for anti-mouse/human/rat EGFR polyclonal	N/A	N/A	WB

Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq.

Description

This is a peptide mapping to a sequence near the carboxy terminus of human EGFR. The EFGR family is a group of four structurally similar tyrosine kinases (EGFR, HER2/neu, ErbB-3, and ErbB-4) that dimerize on binding with a number of ligands, including EGF and transforming growth factor alpha (1&2). The 170 kDa epidermal growth factor receptor binds EGF which activates a tyrosine-specific protein kinase activity intrinsic to the receptor (3&4). Epidermal growth factor receptor overexpression is pronounced in virtually all squamous carcinomas and is also found in > or = 65% of large cell and adenocarcinomas. It is not expressed in situ by small cell lung carcinoma. Overexpression of EGFR is one of the earliest and most consistent abnormalities in bronchial epithelium of high-risk smokers (1).

Applications Reported

For research use only, not for diagnostic or therapeutic use. This blocking peptide has been reported for use in competition studies.

References

1. Franklin WA, Veve R, Hirsch FR, Helfrich BA, Bunn PA Jr. Epidermal growth factor receptor family in lung cancer and premalignancy. Semin Oncol 2002 Feb;29(1 Suppl 4):3-14.
2. Yarden Y. The EGFR family and its ligands in human cancer, signalling mechanisms and therapeutic opportunities. Eur J Cancer 2001 Sep: 37 Suppl 4: S3-8.
3. Reynolds F.H. Jr., Todaro G.J., Fryling C., and Stephenson J.R. Human transforming growth factors induces tyrosine phosphorylation of EGR receptors. Nature 1981 292: 259-262.
4. Chen W.S., Lazar C.S., Poenie M, Tsien R.Y., Gill G.N., Rosenfeld M.G. Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor. Nature 1987 328: 820-823.

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