protein

Recombinant Human Epidermal Growth Factor Receptor-Sf9 (ErbB1)

MBS143248

0.002 mg

140 USD

Recombinant Protein

Recombinant Human Epidermal Growth Factor Receptor-Sf9 (ErbB1)

Epidermal Growth Factor Receptor-Sf9

EGFR Human Sf9; Epidermal Growth Factor Receptor Sf9 Human Recombinant; Epidermal growth factor receptor; EC 2.7.10.1; Receptor tyrosine-protein kinase ErbB-1; ERBB; mENA; ERBB1; EGFR; EGFR Sf9

epidermal growth factor receptor isoform a; Epidermal growth factor receptor; epidermal growth factor receptor; avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; cell growth inhibiting protein 40; cell proliferation-inducing protein 61; erb-b2 receptor tyrosine kinase 1; proto-oncogene c-ErbB-1; receptor tyrosine-protein kinase erbB-1; epidermal growth factor receptor; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1

EGFR

EGFR; EGFR; ERBB; HER1; mENA; ERBB1; PIG61; NISBD2; ERBB; ERBB1; HER1

EGFR_HUMAN

Sf9 Insect Cells

1210

LEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCK LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIAASW SHPQFEK.

Greater than 90.0% as determined by SDS-PAGE.

ErbB1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1x PBS pH-7.4. Sterile Filtered White lyophilized (freeze-dried) powder.

Lyophilized EGFR although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon reconstitution EGFR should be stored at 4 degree C between 2-7 days and for future use below -18 degree C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Solubility: It is recommended to reconstitute the lyophilized EGFR in sterile PBS not less than 100 ug/ml, which can then be further diluted to other aqueous solutions.

PROTEIN KINASES; Enzymes; EGF Receptor

Description: The EGFR contains the extracellular domain of the human EGFR (25-647 a.a.) excluding the signal peptide which is cleaved by the insect cells having an approximate Mw of 85kDa. The EGFR is fused to a C-terminal Strep-tag and purified by proprietary chromatographic techniques. Introduction: The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-?, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

29725609

NP_005219.2

NM_005228.3

P00533

69,228 Da

AGE/RAGE Pathway (698754); Adaptive Immune System Pathway (366160); Adherens Junction Pathway (83070); Adherens Junction Pathway (481); AhR Pathway (755436); Alpha6-Beta4 Integrin Signaling Pathway (198807); Androgen Receptor Signaling Pathway (198806); Arf6 Signaling Events Pathway (138034); Axon Guidance Pathway (105688); Bladder Cancer Pathway (83115)

The protein encoded by this gene is a transmembrane glycoprotein that is a member of the protein kinase superfamily. This protein is a receptor for members of the epidermal growth factor family. EGFR is a cell surface protein that binds to epidermal growth factor. Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. Mutations in this gene are associated with lung cancer. Multiple alternatively spliced transcript variants that encode different protein isoforms have been found for this gene. [provided by RefSeq, Jul 2010]

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, tyrosine (receptor); Tumor suppressor; EC 2.7.10.1; Kinase, protein; Protein kinase, TK; Membrane protein, integral; TK group; EGFR family. Chromosomal Location of Human Ortholog: 7p12. Cellular Component: extracellular space; endoplasmic reticulum membrane; nuclear membrane; focal adhesion; cell surface; basolateral plasma membrane; integral to membrane; lipid raft; Golgi membrane; membrane; perinuclear region of cytoplasm; cytoplasm; apical plasma membrane; plasma membrane; AP-2 adaptor complex; endosome membrane; nucleus; receptor complex; endosome. Molecular Function: identical protein binding; epidermal growth factor receptor activity; epidermal growth factor binding; nitric-oxide synthase regulator activity; transmembrane receptor protein tyrosine kinase activity; receptor signaling protein tyrosine kinase activity; protein phosphatase binding; protein kinase binding; actin filament binding; integrin binding; protein binding; enzyme binding; transmembrane receptor activity; MAP kinase kinase kinase activity; protein heterodimerization activity; protein-tyrosine kinase activity; ubiquitin protein ligase binding; double-stranded DNA binding; chromatin binding; glycoprotein binding; ATP binding. Biological Process: circadian rhythm; diterpenoid metabolic process; positive regulation of nitric oxide biosynthetic process; activation of MAPKK activity; nerve growth factor receptor signaling pathway; alkanesulfonate metabolic process; positive regulation of vasodilation; protein insertion into membrane; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; positive regulation of MAP kinase activity; cell-cell adhesion; positive regulation of fibroblast proliferation; ovulation cycle; cell surface receptor linked signal transduction; hair follicle development; positive regulation of superoxide release; negative regulation of mitotic cell cycle; positive regulation of DNA repair; fibroblast growth factor receptor signaling pathway; digestive tract morphogenesis; response to osmotic stress; phospholipase C activation; response to hydroxyisoflavone; hydrogen peroxide metabolic process; positive regulation of transcription from RNA polymerase II promoter; regulation of nitric-oxide synthase activity; response to oxidative stress; response to calcium ion; negative regulation of protein catabolic process; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; negative regulation of epidermal growth factor receptor signaling pathway; axon guidance; tongue development; embryonic placenta development; peptidyl-tyrosine phosphorylation; translation; positive regulation of smooth muscle cell proliferation; protein amino acid autophosphorylation; signal transduction; positive regulation of synaptic transmission, glutamatergic; learning and/or memory; salivary gland morphogenesis; positive regulation of cell proliferation; response to stress; regulation of peptidyl-tyrosine phosphorylation; epidermal growth factor receptor signaling pathway; ossification; phosphoinositide-mediated signaling; MAPKKK cascade; liver development; positive regulation of protein kinase B signaling cascade; cell proliferation; cerebral cortex cell migration; positive regulation of vasoconstriction; calcium-dependent phospholipase A2 activation; innate immune response; positive regulation of protein amino acid phosphorylation; astrocyte activation; response to cobalamin; positive regulation of DNA replication; positive regulation of phosphorylation; positive regulation of cell migration; lung development; positive regulation of inflammatory response. Disease: Lung Cancer

0.002 mg

140 USD

0.01 mg

205

0.1 mg

755