| Host: |
Insect cells |
| Note: |
STRICTLY FOR FURTHER RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: |
Recombinant-Human EGFR (erbb1)-protein was developed from insect cells. For use in research applications. |
| Conjugation: |
Unconjugated |
| Formulation: |
Lyophilised from 0.2 Mu m filtered 20mM Tris, 50mM NaCl, pH 7.4. |
| Dilution Range: |
A quick spin of the vial followed by reconstitution in sterile PBS pH 7.4 to a concentration not less than 0.1 mg/mL. Solubilize for 1hr at room temp with gentle mixing. |
| Storage Instruction: |
Can be stored in working aliquots at 2°C-8°C C for one month, or at-20°C to-70°C for 1 year.It is recommended to add 0.1% HSA or BSA for long term storage. Avoid repeated freeze/thaw cycles. NA |
| Endotoxin: |
Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg). NA |
| Immunoreactivity: |
The activity was determined by the ability to bind human EGF in functional ELISA. NA |
| Gene Symbol: |
EGFR |
| Gene ID: |
1956 |
| Uniprot ID: |
EGFR_HUMAN |
| Immunogen Region: |
ECD |
| Immunogen: |
DNA sequence encoding extracellular domain of Human EGFR (erbb1) to a C-terminal polyHis tag was expressed in Insect cells. NA |
| Tissue Specificity | Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers. |
| Post Translational Modifications | Phosphorylated on Tyr residues in response to EGF. Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2. Monoubiquitinated and polyubiquitinated upon EGF stimulation.which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126. Ubiquitinated by ZNRF1 or CBL at different lysines in response to EGF stimulation.leading to recruitment of the ESCRT machinery and subsequent degradation in the lysosomes. Deubiquitinated by UCHL1 leading to the inhibition of its degradation. Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling. Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197. |
| Function | Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. 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. May also activate the NF-kappa-B signaling cascade. 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. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. 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. Plays a role in enhancing learning and memory performance. Plays a role in mammalian pain signaling (long-lasting hypersensitivity). Isoform 2 may act as an antagonist of EGF action. (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins. |
| Protein Name | Epidermal Growth Factor ReceptorProto-Oncogene C-Erbb-1Receptor Tyrosine-Protein Kinase Erbb-1 |
| Database Links | Reactome: R-HSA-1227986Reactome: R-HSA-1236382Reactome: R-HSA-1236394Reactome: R-HSA-1250196Reactome: R-HSA-1251932Reactome: R-HSA-1257604Reactome: R-HSA-177929Reactome: R-HSA-179812Reactome: R-HSA-180292Reactome: R-HSA-180336Reactome: R-HSA-182971Reactome: R-HSA-1963640Reactome: R-HSA-1963642Reactome: R-HSA-212718Reactome: R-HSA-2179392Reactome: R-HSA-2219530Reactome: R-HSA-445144Reactome: R-HSA-5637810Reactome: R-HSA-5638303Reactome: R-HSA-5673001Reactome: R-HSA-6785631Reactome: R-HSA-6811558Reactome: R-HSA-8847993Reactome: R-HSA-8856825Reactome: R-HSA-8856828Reactome: R-HSA-8857538Reactome: R-HSA-8863795Reactome: R-HSA-8866910Reactome: R-HSA-9009391Reactome: R-HSA-9013507Reactome: R-HSA-9609690Reactome: R-HSA-9634638Reactome: R-HSA-9664565Reactome: R-HSA-9665348Reactome: R-HSA-9665686 |
| Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinEndoplasmic Reticulum MembraneGolgi Apparatus MembraneNucleus MembraneEndosomeEndosome MembraneNucleusIn Response To EgfTranslocated From The Cell Membrane To The Nucleus Via Golgi And ErEndocytosed Upon Activation By LigandColocalized With Gper1 In The Nucleus Of Estrogen Agonist-Induced Cancer-Associated Fibroblasts (Caf)Isoform 2: Secreted |
| Alternative Protein Names | Epidermal Growth Factor Receptor proteinProto-Oncogene C-Erbb-1 proteinReceptor Tyrosine-Protein Kinase Erbb-1 proteinEGFR proteinERBB proteinERBB1 proteinHER1 protein |
Information sourced from Uniprot.org
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