04-283
Anti-phospho-EGFR (Tyr845) Antibody, clone 12A3
clone 12A3, Upstate®, from mouse
Synonym(s):
ERBB, ERBB1
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
12A3, monoclonal
species reactivity
human, mouse
manufacturer/tradename
Upstate®
technique(s)
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
phosphorylation (pTyr845)
Gene Information
human ... EGFR(1956)
mouse ... Egfr(13649)
Related Categories
Specificity
Recognizes phosphorylated EGFR on Tyrosine 845.
Immunogen
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
Quality
Routinely evaluated by immunoblot.
Target description
180 kDa
Physical form
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
Storage and Stability
2 years at -20°C from date of shipment
Analysis Note
Control
Includes EGF treated Hep2G cell lysate as a positive control
Includes EGF treated Hep2G cell lysate as a positive control
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
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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Storage Class Code
10 - Combustible liquids
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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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