Egfr (P1116) Blocking Peptide | Egfr blocking peptide

Mouse Egfr Blocking Peptide (P1116)

• Gene Names: Egfr; Wa5; wa2; Erbb; Errp; wa-2; Errb1; AI552599; 9030024J15Rik
• Synonyms: Egfr (P1116); Mouse Egfr Blocking Peptide (P1116); Epidermal growth factor receptor; Egfr; Egfr blocking peptide

• Specificity: The synthetic peptide sequence is selected from aa 1116-1150 of HUMAN Egfr
• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 1210

• 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. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) (By similarity).
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for Egfr blocking peptide

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, amphiregulin, 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.

NCBI and Uniprot Product Information

• NCBI GI #: 1352359
• NCBI GeneID: 13649
• UniProt Accession #: Q01279
• Molecular Weight: 134,853 Da
• NCBI Official Full Name: Epidermal growth factor receptor
• NCBI Official Synonym Full Names: epidermal growth factor receptor
• NCBI Official Symbol: Egfr
• NCBI Official Synonym Symbols: Wa5; wa2; Erbb; Errp; wa-2; Errb1; AI552599; 9030024J15Rik
• NCBI Protein Information: epidermal growth factor receptor
• UniProt Protein Name: Epidermal growth factor receptor
• Protein Family: Epidermal growth factor receptor
• UniProt Gene Name: Egfr
• UniProt Entry Name: EGFR_MOUSE

Uniprot Description

EGFR: a receptor tyrosine kinase. This is a receptor for epidermal growth factor (EGF) and related growth factors including TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30, and vaccinia virus growth factor. EGFR is involved in the control of cell growth and differentiation. It is a single-pass transmembrane tyrosine kinase. Ligand binding to this receptor results in receptor dimerization, autophosphorylation (in trans), activation of various downstream signaling molecules and lysosomal degradation. It can be phosphorylated and activated by Src. Activated EGFR binds the SH2 domain of phospholipase C-gamma (PLC-gamma), activating PLC-gamma-mediated downstream signaling. Phosphorylated EGFR binds Cbl, leading to its ubiquitination and degradation. Grb2 and SHC bind to phospho-EGFR and are involved in the activation of MAP kinase signaling pathways. Phosphorylation on Ser and Thr residues is thought to represent a mechanism for attenuation of EGFR kinase activity. EGFR is overexpressed in breast, head and neck cancers, correlating with poor survival. Activating somatic mutations are seen in lung cancer, corresponding to the minority of patients with strong responses to the EGFR inhibitor Iressa (gefitinib). Mutations and amplifications are also seen in glioblastoma, and upregulation is seen in colon cancer and neoplasms. In xenografts, inhibitors synergize with cytotoxic drugs in the inhibition of many tumor types. Inhibitors include: Iressa/ZD1839, Erbitux, Tarceva, and lapatinib. Four alternatively spliced isoforms have been described.

Protein type: Protein kinase, TK; Protein kinase, tyrosine (receptor); Membrane protein, integral; EC 2.7.10.1; Kinase, protein; Tumor suppressor; TK group; EGFR family

Cellular Component: apical plasma membrane; basolateral plasma membrane; cell surface; cytoplasm; early endosome membrane; endocytic vesicle; endosome; endosome membrane; focal adhesion; intracellular; lipid raft; membrane; nucleus; perinuclear region of cytoplasm; plasma membrane; receptor complex; synapse

Molecular Function: actin filament binding; calmodulin binding; chromatin binding; enzyme binding; epidermal growth factor binding; epidermal growth factor receptor activity; glycoprotein binding; identical protein binding; integrin binding; kinase activity; nitric-oxide synthase regulator activity; protein binding; protein heterodimerization activity; protein kinase binding; protein phosphatase binding; protein-tyrosine kinase activity; receptor binding; signal transducer activity; transmembrane receptor activity; ubiquitin protein ligase binding

Biological Process: activation of MAPKK activity; astrocyte activation; cell morphogenesis; cell proliferation; cell surface receptor linked signal transduction; cell-cell adhesion; cerebral cortex cell migration; digestive tract morphogenesis; embryonic placenta development; epidermal growth factor receptor signaling pathway; epidermis development; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; hair follicle development; learning and/or memory; negative regulation of apoptosis; negative regulation of mitotic cell cycle; negative regulation of protein catabolic process; neurite morphogenesis; ovulation cycle; peptidyl-tyrosine phosphorylation; positive regulation of bone resorption; positive regulation of cell growth; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of DNA repair; positive regulation of DNA replication; positive regulation of epithelial cell proliferation; positive regulation of fibroblast proliferation; positive regulation of inflammatory response; positive regulation of MAP kinase activity; positive regulation of nitric oxide biosynthetic process; positive regulation of phosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of smooth muscle cell proliferation; positive regulation of superoxide release; positive regulation of synaptic transmission, glutamatergic; positive regulation of transcription from RNA polymerase II promoter; positive regulation of vasoconstriction; positive regulation of vasodilation; protein amino acid autophosphorylation; regulation of cell proliferation; regulation of nitric-oxide synthase activity; regulation of peptidyl-tyrosine phosphorylation; response to calcium ion; salivary gland morphogenesis; signal transduction; translation; wound healing