04-283
Anti-phospho-EGFR (Tyr845) Antibody, clone 12A3
clone 12A3, Upstate®, from mouse
Sinónimos:
ERBB, ERBB1
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100 μG
479,00 €
479,00 €
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100 μG
479,00 €
About This Item
Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
479,00 €
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origen biológico
mouse
Nivel de calidad
forma del anticuerpo
purified antibody
tipo de anticuerpo
primary antibodies
clon
12A3, monoclonal
reactividad de especies
human, mouse
fabricante / nombre comercial
Upstate®
técnicas
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotipo
IgG1
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
wet ice
modificación del objetivo postraduccional
phosphorylation (pTyr845)
Información sobre el gen
human ... EGFR(1956)
mouse ... Egfr(13649)
Especificidad
Recognizes phosphorylated EGFR on Tyrosine 845.
Inmunógeno
KLH-conjugated synthetic peptide encompassing the surrounding amino acids of Tyr 845 in human EGFR.
Aplicación
Detect phospho-EGFR (Tyr845) using this Anti-phospho-EGFR (Tyr845) Antibody, clone 12A3 validated for use in ELISA, IC, IP & WB.
Research Category
Signaling
Signaling
Research Sub Category
Growth Factors & Receptors
Growth Factors & Receptors
Calidad
Routinely evaluated by immunoblot.
Descripción de destino
180 kDa
Forma física
100 µg of mouse monoclonal IgG1 lyophilized in 2X PBS containing 0.09% sodium azide, PEG, and sucrose
Format: Purified
Subsequent thiophilic adsorption and size exclusion chromatography
Almacenamiento y estabilidad
2 years at -20°C from date of shipment
Nota de análisis
Control
Includes EGF treated Hep2G cell lysate as a positive control
Includes EGF treated Hep2G cell lysate as a positive control
Información legal
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Cláusula de descargo de responsabilidad
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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Código de clase de almacenamiento
10 - Combustible liquids
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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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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