- CITATIONS: 2
|Application ||DB, E|
|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||This EGFR Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding Y1125 of human EGFR.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-EGFR(Y1125) Antibody 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). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). 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.|
Provided below are standard protocols that you may find useful for product applications.
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.
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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