EGFR / HER1 / ErbB1 recombinant protein

Recombinant Mouse EGFR / HER1 / ErbB1 Protein (Fc tag)

Cat. Num. AAA2546669

• Gene Names: Egfr; Wa5; wa2; Erbb; Errp; wa-2; Errb1; AI552599; 9030024J15Rik
• Purity: > 90 % as determined by SDS-PAGE
• Synonyms: EGFR / HER1 / ErbB1; Recombinant Mouse EGFR / HER1 / ErbB1 Protein (Fc tag); RP23-295E4.1; 9030024J15Rik; AI552599; Erbb; Errp; Wa5; wa-2; wa2; EGFR / HER1 / ErbB1 recombinant protein

• Host: Human Cells
• Purity/Purification: > 90 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 1210

• Application Notes: The secreted recombinant mouse EGFR/Fc is a disulfide-linked homodimer. The reduced monomer comprises 864 amino acids and has a calculated molecular mass of 96 kDa. As a result of glycosylation, the apparent molecular mass of rmEGFR/Fc monomer is approximately 130 kDa in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Leu 25
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for EGFR / HER1 / ErbB1 recombinant protein

Background: As a member of the epidermal growth factor receptor (EGFR) family, EGFR protein is type I transmembrane glycoprotein that binds a subset of EGF family ligands including EGF, amphiregulin, TGF-alpha, betacellulin, etc. EGFR protein plays a crucial role in signaling pathway in the regulation of cell proliferation, survival and differentiation. Binding of a ligand induces EGFR protein homo- or heterodimerization, the subsequent tyrosine autophosphorylation and initiates various down stream pathways (MAPK, PI3K/PKB and STAT). In addition, EGFR signaling also has been shown to exert action on carcinogenesis and disease progression, and thus EGFR protein is proposed as a target for cancer therapy currently.

Description: A DNA sequence encoding the extracellular domain of mouse EGFR (Q01279) (Met 1-Ser 647) was fused with the Fc region of human IgG1 at the C-terminus.

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: 134,853 Da
• 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
• UniProt Gene Name: Egfr

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

Chromosomal Location of Human Ortholog: 11 A2|11 9.41 cM

Cellular Component: apical plasma membrane; basolateral plasma membrane; cell surface; cell-cell adherens junction; 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; receptor-mediated endocytosis; 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