Recombinant human EGFR (A767-S768insTLA) protein (Active)
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Recombinant human EGFR (A767-S768insTLA) protein (Active) is a Human Fragment protein, in the 668 to 1210 aa range, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, FuncS.
View Alternative Names
ERBB, ERBB1, HER1, EGFR, Epidermal growth factor receptor, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1
- FuncS
Supplier Data
Functional Studies - Recombinant human EGFR (A767-S768insTLA) protein (Active) (AB268457)
The specific activity of ab268457 was 27 nmol/min/mg in a peptide kinase assay using Poly (4 : 1, Glu, Tyr) as substrate.
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human EGFR (A767-S768insTLA) protein (Active) (AB268457)
SDS-PAGE analysis of ab268457.
Reactivity data
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Why is this recommended?
We recommend this product because it’s often used in the same experiment or related research.
We advise that you always check the datasheet to ensure it fits your experiments, or contact ourtechnical teamfor help.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The EGFR protein plays an important role in cellular communication and signaling processes. EGFR pairs with other receptor family members to form active dimers or even higher-order complexes which in turn initiate intracellular signaling cascades. Through these complexes EGFR influences many processes including cell differentiation and repair. This function of EGFR makes it an integral part of mammalian biology affecting how cells respond to their environment by mediating changes in gene expression.
Pathways
EGFR is a central player in the MAPK and PI3K/Akt signaling pathways. Alongside other protein partners like KRAS and PI3 kinase it contributes to transmitting signals from the cell surface to the nucleus affecting gene transcription and cell behavior. These pathways are important for normal cell growth and division and aberrations in these pathways can lead to excessive or insufficient cell proliferation.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
The protein expressed by the EGFR gene functions as a receptor tyrosine kinase, binding with ligands from the EGF family to activate several signaling cascades that translate extracellular signals into cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen, BTC/betacellulin, epiregulin, and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation, recruiting adapter proteins like GRB2 and activating complex downstream signaling pathways such as RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STATs, and possibly the NF-kappa-B cascade. EGFR also directly phosphorylates proteins like RGS16 and MUC1, influencing various cellular processes including its coupling with G protein-coupled receptor signaling and cell migration through interaction with CCDC88A/GIV. Isoform 2 of EGFR may act as an antagonist to EGF actions. In microbial infection, EGFR also serves as a receptor facilitating hepatitis C virus (HCV) entry into hepatocytes by promoting CD81-CLDN1 receptor complexes and enhancing membrane fusion with HCV envelope glycoproteins. This supplementary information is collated from multiple sources and compiled automatically.
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.
Post-translational modifications
Phosphorylated on Tyr residues in response to EGF (PubMed:20462955, PubMed:27153536). 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 (PubMed:27153536). 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 (By similarity). 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 (PubMed:33996800). Deubiquitinated by UCHL1 leading to the inhibition of its degradation (By similarity).. 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.
Subcellular localisation
Nucleus membrane
Product protocols
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Target data
Product promise
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