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Wählen Sie konfigurierbare Panels & Premixed-Kits - ODER - Kits für die zelluläre Signaltransduktion & MAPmates™
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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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This Anti-phospho-EGFR (Tyr1148) Antibody is validated for use in WB for the detection of phospho-EGFR (Tyr1148).
More>>This Anti-phospho-EGFR (Tyr1148) Antibody is validated for use in WB for the detection of phospho-EGFR (Tyr1148). Less<<
Anti-phospho-EGFR (Tyr1148) Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
FUNCTION: SwissProt: P00533 # Isoform 2/truncated isoform may act as an antagonist. SIZE: 1210 amino acids; 134277 Da SUBUNIT: Binds RIPK1. CBL interacts with the autophosphorylated C- terminal tail of the EGF receptor. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. The autophosphorylated form interacts with PIK3C2B, maybe indirectly. Interacts with PELP1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. & Isoform 2: Secreted. TISSUE SPECIFICITY: Expressed in placenta. Isoform 2 is also expressed in ovarian cancers. PTM: Phosphorylation of Ser-695 is partial and occurs only if Thr- 693 is phosphorylated. & Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occur.DISEASE:SwissProt: P00533 # Defects in EGFR are associated with lung cancer [MIM:211980]. SIMILARITY: SwissProt: P00533 ## Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily. & Contains 1 protein kinase domain. MISCELLANEOUS: Binding of EGF to the receptor leads to dimerization, internalization of the EGF-receptor complex, induction of the tyrosine kinase activity, stimulation of cell DNA synthesis, and cell proliferation.
Molecular Weight
185 kDa
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Dimensions
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Safety Information according to GHS
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Product Usage Statements
Quality Assurance
Routinely evaluated by immunoblot.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 2 years at -20°C from date of shipment. Handling Recommendations: Upon first thaw, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerolcontaining solutions to become frozen during storage.
Amphiregulin induces tyrosine phosphorylation of the epidermal growth factor receptor and p185erbB2. Evidence that amphiregulin acts exclusively through the epidermal growth factor receptor at the surface of human epithelial cells. Johnson, G R, et al. J. Biol. Chem., 268: 2924-31 (1993)
1992
The COOH-terminal half of the amphiregulin (AR) molecule has sequence homology to epidermal growth factor (EGF). The ability of AR to elicit in vivo phosphorylation of the EGF receptor (EGFR) and p185erbB2 was studied in four human epithelial cell lines which expressed either or both of the receptor tyrosine kinases. AR induced the phosphorylation of the EGFR and p185erbB2, and phosphoamino acid analysis revealed enhanced phosphorylation of tyrosine residues in both receptor proteins. A monoclonal antibody (mAb) which binds to the extracellular domain of the EGFR blocked the phosphorylation of the EGFR and p185erbB2 as well as AR-induced mitogenesis indicating that the EGFR mediated these responses. In MDA-MB-453 cells which lack EGFRs, AR did not induce phosphorylation of p185erbB2, did not affect proliferation, and had no detectable effect on the phosphorylation of cellular proteins isolated using an anti-phosphotyrosine mAb. Qualitatively, in vivo phosphorylations induced by AR and EGF were found to be indistinguishable as demonstrated by analysis of cellular 32P-labeled proteins isolated with the anti-phosphotyrosine mAb. Moreover, in the presence of the anti-EGFR mAb, AR had no effect on the proliferation of cells. These results provide strong evidence that the EGFR is the sole cell surface mediator of the action of AR in human epithelial cells.
The ability of different Fc receptors (Fc gamma R) on IgG-mediated cytotoxicity for human epidermoid carcinoma A431 cells bearing large number of epidermal growth factor receptors (EGFRs) was examined by using two isotypes (IgG1 and IgG2a) of murine monoclonal antibodies (MoAbs) against EGFR in the presence of human monocytes and granulocytes. Two MoAbs (225 and LA1) of the IgG1 isotype exhibited effective cytolytic activity for A431 cells with human polymorphonuclear leukocytes (PMN) rather than with human mononuclear cells (MNC). In contrast, two MoAbs (528 and 579) of the IgG2a-isotype lysed the cells less effectively with PMN than with MNC. Anti-Fc gamma R II (CDw32) MoAb 2E1 inhibited the IgG1-mediated cytotoxicity by PMN, and anti-Fc gamma R III (CD16) MoAb 80H3 did not inhibit the IgG2a-mediated cytotoxicity by MNC. Under these conditions, antibody-dependent cell-mediated cytotoxicity by mouse MoAb IgG1 isotypes resulted from antibody binding to the Fc gamma R II (CDw32) of PMN.
Elevated expression of the receptor for epidermal growth factor (EGF) is a characteristic of several malignancies including those of the breast, bladder, prostate, lung, and neuroglia. To therapeutically target the cytotoxic action of diphtheria toxin to EGF receptor-expressing tumor cells, we have constructed a hybrid gene in which the sequences for the binding domain of diphtheria toxin have been replaced by those for human EGF. The resulting fusion toxins, DAB486EGF and DAB389EGF, bind specifically to the EGF receptor and inhibit protein synthesis in a variety of EGF receptor expressing human tumor cell lines with an IC50 as low as 0.1 pM. Comparisons of DAB486EGF and DAB389EGF showed that DAB389EGF was consistently 10- to 100-fold more cytotoxic than DAB486EGF. Like diphtheria toxin, the cytotoxic action of DAB389EGF results from ADP-ribosylation of elongation factor-2 and is sensitive to the action of chloroquine. Studies of the kinetics of cellular intoxication showed that a 15-min exposure of EGF receptor-expressing A431 cells to DAB389EGF results in complete protein synthesis inhibition within 4 h. Furthermore, inhibition of protein synthesis results in elimination of human tumor cell colonies. These findings show that DAB389EGF is a potential therapeutic agent for a wide variety of EGF receptor-expressing solid tumors.
Millipore’s EGFR (Epidermal growth factor receptor) antibodies, kits, and proteins are high quality, validated tools for EGFR research. See below for a selection of EGFR and phospho-EGFR products. Weitere Informationen >>
