04-283
Anti-phospho-EGFR (Tyr845) Antibody, clone 12A3
clone 12A3, Upstate®, from mouse
Synonyme(s) :
ERBB, ERBB1
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About This Item
Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41
Source biologique
mouse
Niveau de qualité
Forme d'anticorps
purified antibody
Type de produit anticorps
primary antibodies
Clone
12A3, monoclonal
Espèces réactives
human, mouse
Fabricant/nom de marque
Upstate®
Technique(s)
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
Isotype
IgG1
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
wet ice
Modification post-traductionnelle de la cible
phosphorylation (pTyr845)
Informations sur le gène
human ... EGFR(1956)
mouse ... Egfr(13649)
Spécificité
Recognizes phosphorylated EGFR on Tyrosine 845.
Immunogène
KLH-conjugated synthetic peptide encompassing the surrounding amino acids of Tyr 845 in human EGFR.
Application
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
Qualité
Routinely evaluated by immunoblot.
Description de la cible
180 kDa
Forme physique
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
Stockage et stabilité
2 years at -20°C from date of shipment
Remarque sur l'analyse
Control
Includes EGF treated Hep2G cell lysate as a positive control
Includes EGF treated Hep2G cell lysate as a positive control
Informations légales
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Clause de non-responsabilité
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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Code de la classe de stockage
10 - Combustible liquids
Certificats d'analyse (COA)
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
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.
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
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
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
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.
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