04-283
Anti-phospho-EGFR (Tyr845) Antibody, clone 12A3
clone 12A3, Upstate®, from mouse
Synonym(e):
ERBB, ERBB1
Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise
Alle Fotos(2)
About This Item
UNSPSC-Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Biologische Quelle
mouse
Qualitätsniveau
Antikörperform
purified antibody
Antikörper-Produkttyp
primary antibodies
Klon
12A3, monoclonal
Speziesreaktivität
human, mouse
Hersteller/Markenname
Upstate®
Methode(n)
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
Isotyp
IgG1
NCBI-Hinterlegungsnummer
UniProt-Hinterlegungsnummer
Versandbedingung
wet ice
Posttranslationale Modifikation Target
phosphorylation (pTyr845)
Angaben zum Gen
human ... EGFR(1956)
mouse ... Egfr(13649)
Spezifität
Recognizes phosphorylated EGFR on Tyrosine 845.
Immunogen
KLH-conjugated synthetic peptide encompassing the surrounding amino acids of Tyr 845 in human EGFR.
Anwendung
Research Category
Zelluläre Signaltransduktion
Zelluläre Signaltransduktion
Research Sub Category
Wachstumsfaktoren & -rezeptoren
Wachstumsfaktoren & -rezeptoren
Detect phospho-EGFR (Tyr845) using this Anti-phospho-EGFR (Tyr845) Antibody, clone 12A3 validated for use in ELISA, IC, IP & WB.
Qualität
Routinely evaluated by immunoblot.
Zielbeschreibung
180 kDa
Physikalische Form
Subsequent thiophilic adsorption and size exclusion chromatography
100 µg of mouse monoclonal IgG1 lyophilized in 2X PBS containing 0.09% sodium azide, PEG, and sucrose
Format: Purified
Lagerung und Haltbarkeit
2 years at -20°C from date of shipment
Hinweis zur Analyse
Control
Includes EGF treated Hep2G cell lysate as a positive control
Includes EGF treated Hep2G cell lysate as a positive control
Rechtliche Hinweise
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Haftungsausschluss
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.
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Lagerklassenschlüssel
10 - Combustible liquids
Analysenzertifikate (COA)
Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.
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Laura Moro et al.
The Journal of biological chemistry, 277(11), 9405-9414 (2002-01-05)
Integrin-mediated cell adhesion cooperates with growth factor receptors in the control of cell proliferation, cell survival, and cell migration. One mechanism to explain these synergistic effects is the ability of integrins to induce phosphorylation of growth factor receptors, for instance
Kyung Lock Kim et al.
ACS central science, 4(5), 614-623 (2018-05-29)
Combinatorial post-translational modifications (PTMs), which can serve as dynamic "molecular barcodes", have been proposed to regulate distinct protein functions. However, studies of combinatorial PTMs on single protein molecules have been hindered by a lack of suitable analytical methods. Here, we
Julie L Boerner et al.
Molecular and cellular biology, 24(16), 7059-7071 (2004-07-30)
When co-overexpressed, the epidermal growth factor receptor (EGFR) and c-Src cooperate to cause synergistic increases in EGF-induced DNA synthesis, soft agar colony growth, and tumor formation in nude mice. This synergy is dependent upon c-Src-mediated phosphorylation of a unique tyrosine
Kyung Lock Kim et al.
Nature communications, 7, 11107-11107 (2016-03-25)
Post-translational modifications (PTMs) of receptor tyrosine kinases (RTKs) at the plasma membrane (PM) determine the signal transduction efficacy alone and in combination. However, current approaches to identify PTMs provide ensemble results, inherently overlooking combinatorial PTMs in a single polypeptide molecule.
J S Biscardi et al.
The Journal of biological chemistry, 274(12), 8335-8343 (1999-03-13)
Accumulating evidence indicates that interactions between the epidermal growth factor receptor (EGFR) and the nonreceptor tyrosine kinase c-Src may contribute to an aggressive phenotype in multiple human tumors. Previous work from our laboratory demonstrated that murine fibroblasts which overexpress both
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