Epidermal growth factor receptor (EGFR) is a transmembrane protein and a member of a family of receptor tyrosine kinases (RTK) called avian erythroblastosis oncogene (BErbB). It contains a ligand-binding domain in its extracellular region, one transmembrane domain, and a tyrosine kinase-containing domain in its cytosolic region. EGFR is encoded by the gene mapped to human chromosome 7p11.2.

EGFR Active human has been used in:

• photo-cross-linking assays
• StavroX cross-linking site identification
• in vitro kinase assay

Epidermal growth factor receptor (EGFR) functions as a receptor for EGF-family of proteins, which are peptide growth factors. EGFR and ligand play a crucial role early embryonic development and in the renewal of stem cells in tissues such as the gut, liver and skin. This receptor-ligand system is also involved in the pathogenesis and progression of various types of carcinomas. In cancer, EGFR pathways promotes cellular proliferation, angiogenesis, metastasis and apoptosis. The microRNA miR-218-5p interacts with and controls EGFR, and in non-small cell lung cancer (NSCLC), the levels of EGFR are inversely related to miR-218-5p. miR-218-5p inhibits proliferation and migration of lung cancer cells by binding with EGFR, and thus, has potential in future NSCLC therapies.

One unit is defined as the amount of enzyme that will phosphorylate 1 pmol of Tyr substrate per minute at pH 7.4 and 30°C.

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol, 10 mM glutathione and 3 mM DTT.

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.