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Rabbit Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IF |
|---|---|
| Primary Accession | P00533 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Monoclonal |
| Clone Names | EP774Y |
| Calculated MW | 134277 Da |
| Gene ID | 1956 |
| 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 phospho-peptide corresponding to residues surrounding Tyr1068 of human EGF receptor was used as immunogen. |
| Dilution | WB~~1:500~5000 IHC~~1:250~500 |
| 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 (pY1068) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | EGFR |
|---|---|
| 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.
Background
Epidermal growth factor receptor (EGFR) is a 170 kDa transmembrane glycoprotein receptor tyrosine kinase that, when activated by epidermal growth factor (EGF), affects cell growth and differentiation in normal and cancer cells (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). EGFR overexpression is exhibited in various cancers, such as glioma, colorectal carcinoma, breast carcinoma, and head and neck carcinoma (4). The phosphorylation level of EGFR is considered one of the important predictors of clinical outcome in non-small cell lung cancer therapy (5).
References
1. Hunter T. et al. Nature 311: 414
2. Reynolds FH, et al. Nature 292: 259
3. Helin K, et al. Oncogene 6: 825
4. Christensen ME, et al. Danish Med Bull 45(2):121-134, 1998.
5. Kanematsu T, et al. Oncol Res 13(5):289-298, 2003
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