ErbB1/EGFR Active Protein | EGFR active protein

Human CellExp ErbB1 / EGFR, mouse recombinant

Cat. Num. AAA845092

• Gene Names: Egfr; Wa5; wa2; Erbb; Errp; wa-2; Errb1; AI552599; 9030024J15Rik
• Applications: SDS-Page
• Purity: >=95%
• Synonyms: ErbB1/EGFR; Human CellExp ErbB1 / EGFR; mouse recombinant; EGFR; ERBB; ERBB1; HER1; PIG61; mENA; EGFR active protein

• Host: HEK293 cells
• Purity/Purification: >=95%
• Form/Format: Lyophilized from 0.22 mum filtered solution in PBS, pH7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.; Appearance: Lyophilized
• Sequence Length: 1210

• Applicable Applications for EGFR active protein: SDS-PAGE
• Solubility/Reconstitution Instructions: Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 ug/ml. Do not vortex. This solution can be stored at 2-8 degree C for up to 1 month. For extended storage, it is recommended to store at -20 degree C.
• Endotoxin Level: <1 EU/mug by LAL method
• Biological Activity: Measured by its binding ability in a functional ELISA. Immobilized mouse EGF at 10 mug/ml can bind mouse EGFR with a linear range of 2.5-1000 ng/ml.
• Results: Measured by its binding ability in a functional ELISA. Immobilized mouse EGF at 10 mug/ml can bind mouse EGFR with a linear range of 2.5-1000 ng/ml.
• Handling: Centrifuge the vial prior to opening.
• Preparation and Storage: At -20 degree C; Shelf Life: 12 months

Testing Data

Related Product Information for EGFR active protein

Background: The epidermal growth factor receptor (EGFR; ErbB-1; HER1) is the cell-surface receptor for members of the epidermal growth factor family (EGF-family) of extracellular protein ligands. The epidermal growth factor receptor is a member of the ErbB family of receptors, a subfamily of four closely related receptor tyrosine kinases: EGFR (ErbB-1), HER2/c-neu (ErbB-2), Her 3 (ErbB-3) and Her 4 (ErbB-4). Mutations affecting EGFR expression or activity could result in cancer.

Product Categories/Family for EGFR active protein

Proteins and Enzymes; Human cell expressed recombinant proteinsCytokines; Growth Factors & Hormones; Human cell expressed recombinant proteinsCytokines; Growth Factors & Hormones; EGFsCytokines; Growth Factors & Hormones; Cytokines & Growth Factors (A-Z)

NCBI and Uniprot Product Information

• NCBI GI #: 46560582
• NCBI GeneID: 13649
• NCBI Accession #: NP_997538.1
• NCBI GenBank Nucleotide #: NM_207655.2
• UniProt Accession #: Q01279
• Molecular Weight: This protein has a C-terminal 6×His tag and has a calculated MW of 70 kDa. The predicted N-terminus is Leu 25. In DTT-reduced SDS-PAGE, protein migrates as 110-115 kDa.
• NCBI Official Full Name: epidermal growth factor receptor isoform 1
• 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: Kinase, protein; Tumor suppressor; Protein kinase, TK; Membrane protein, integral; EC 2.7.10.1; Protein kinase, tyrosine (receptor); TK group; EGFR family

Cellular Component: Golgi apparatus; focal adhesion; cell surface; endoplasmic reticulum; basolateral plasma membrane; integral to membrane; lipid raft; membrane; perinuclear region of cytoplasm; endocytic vesicle; apical plasma membrane; cytoplasm; plasma membrane; endosome membrane; intracellular; nucleus; endosome; receptor complex

Molecular Function: identical protein binding; epidermal growth factor receptor activity; epidermal growth factor binding; nitric-oxide synthase regulator activity; nucleotide binding; transmembrane receptor protein tyrosine kinase activity; receptor signaling protein tyrosine kinase activity; protein kinase binding; protein phosphatase binding; protein kinase activity; transferase activity; actin filament binding; integrin binding; protein binding; signal transducer activity; enzyme binding; transmembrane receptor activity; protein heterodimerization activity; protein-tyrosine kinase activity; ubiquitin protein ligase binding; transferase activity, transferring phosphorus-containing groups; chromatin binding; kinase activity; glycoprotein binding; ATP binding; receptor binding

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