|Application ||WB, FC|
|Calculated MW||134277 Da|
|Other Names||Epidermal growth factor receptor, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1, EGFR, ERBB, ERBB1, HER1|
|Target/Specificity||A synthetic peptide corresponding to residues in the extracellular domain near N-terminus of human EGFR was used as immunogen. The antibody does not cross-react with other ERBB family members. Predicted to cross-react with rat, pig and bovine, based on sequence homology.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||EGFR Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||ERBB, ERBB1, HER1|
|Function||Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536, PubMed:20837704). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS- RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Plays a role in enhancing learning and memory performance (By similarity).|
|Cellular Location||Cell membrane; Single- pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome. Endosome membrane. Nucleus. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER (PubMed:20674546). Endocytosed upon activation by ligand (PubMed:2790960, PubMed:17182860, PubMed:27153536). Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer- associated fibroblasts (CAF) (PubMed:20551055)|
|Tissue Location||Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers.|
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Provided below are standard protocols that you may find useful for product applications.
Epidermal growth factor receptor (EGFR) is a 170 kDa transmembrane glycoprotein receptor tyrosine kinase that, activated by epidermal growth factor (EGF), affects cell growth and differentiation (1). Binding of EGF or TGF alpha to EGFR activates tyrosine kinase activity of the receptor (2). The carboxy terminal tyrosine residues on EGFR, Tyr 1068, Tyr 1148, and Tyr 1173, are the major sites of autophosphorylation, which occurs as a result of EGF binding (3). Once activated, EGFR phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR. Another autophosphorylation site, Tyr 1086, is situated within the cytoplasmic domain, and is phosphorylated to a higher extent by c-Src than by EGFR (4).
1. Hunter, T. The epidermal growth factor receptor gene and its product. Nature 311: 414
2. Reynolds, F.H. Jr., et al. Human transforming growth factors induces tyrosine phosphorylation of EGF receptors. Nature 292: 259
3. Helin, K., et al. The biological activity of the human epidermal growth factor receptor is positively regulated by its C-terminal tyrosines. Oncogene 6: 825
4. Lombardo, C.R., et al. In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites. Biochemistry 34: 16456
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