|Application ||WB, IF|
|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 phospho specific peptide corresponding to residues surrounding tyrosine 845 of human EGFR was used as an immunogen. This antibody detects EGFR phosphorylated on tyrosine 845|
|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 Phospho (pY845) 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 175 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 epidermal growth factor (EGF) receptor is regulated by EGF-stimulated autophosphorylation and by phorbol ester-stimulated, protein kinase C (Ca2+/phospholipid-dependent enzyme) mediated phosphorylation at identified sites. Analysis of predicted secondary structure of the EGF receptor reveals that all of the phosphorylation sites are located near beta turns (3). I t has been reported that stimulating human glioblastoma cells with recombinant HGF induces biologically relevant EGFR activation. EGFR phosphorylation at Tyr(845) and Tyr(1068) increased 6 to 24 h after cell stimulation with HGF and temporally coincided with the induction of transforming growth factor-alpha (~5-fold) and HB-EGF (~23-fold) expression. Tyr(845) and Tyr(1068) phosphorylation, in response to HGF, was inhibited by cycloheximide and actinomycin D, consistent with a requirement for DNA transcription and RNA translation (4).
1. Hunter, T. et al. Nature 311: 414-416 (1984). 2. Reynolds, F.H. Jr., et al. Nature 292: 259-262 (1981). 3. Heisermann GJ et al. J Biol Chem 263(26):14152-8, 1988. 4. Reznik TE, et al. Mol Cancer Res 6(1): 139-50, 2008.
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