EGFR Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IP |
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Primary Accession | P00533 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 134277 Da |
Gene ID | 1956 |
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Application & Usage | Western blotting (1:500 – 1:2500) and Immunoprecipitation. However, the optimal concentrations should be determined individually. The antibody recognizes the EGFR of human and mouse origins. Reactivity to other species has not been tested. |
Other Names | EGFR, Epidermal Growth Factor Receptor, ERBB, ERBB1, ERBB-1, Erythroblastic Leukemia viral (v-erb-b) oncogene homolog |
Target/Specificity | EGFR |
Antibody Form | Liquid |
Appearance | Colorless liquid |
Formulation | 100 µl affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 30% glycerol, 0.5% BSA and 0.01% thimerosal. |
Handling | The antibody solution should be gently mixed before use. |
Reconstitution & Storage | -20 °C |
Background Descriptions | |
Precautions | EGFR Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | EGFR (HGNC:3236) |
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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, PubMed:17909029). 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). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (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, PubMed:17909029). Endocytosed upon activation by ligand (PubMed:2790960, PubMed:17182860, PubMed:27153536, PubMed:17909029). 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
The EGF receptor family comprises several related receptor tyrosine kinases that are frequently overexpressed in a variety of carcinomas. Members of this receptor family include EGFR (HER1), Neu (ErbB-2, HER2), ErbB-3 (HER3) and ErbB-4 (HER4), which form either homodimers or heterodimers upon ligand binding. Exons in the EGFR gene product are frequently either deleted or duplicated to produce deletion mutants (DM) or tandem duplication mutants (TDM), respectively, which are detected at various molecular weights. EGFR binds several ligands, including epidermal growth factor (EGF), transforming growth factor α (TGFα), Amphiregulin and heparin binding-EGF (HB-EGF). Ligand binding promotes the internalization of EGFR via Clathrin-coated pits and its subsequent degradation in response to its intrinsic tyrosine kinase. EGFR is involved in organ morphogenesis and maintenance and repair of tissues, but upregulation of EGFR is associated with tumor progression. The oncogenic effects of EGFR include initiation of DNA synthesis, enhanced cell growth, invasion and metastasis. Abrogation of EGFR results in cell cycle arrest, apoptosis or dedifferentiation of cancer cells, suggesting that EGFR may be an effective therapeutic target.
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