E6154
Anti-phospho-Epidermal Growth Factor Receptor (pTyr1068) antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-phospho-EGFR (pTyr1068)
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About This Item
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous glycerol solution
mol wt
antigen 170 kDa
species reactivity
human, rat
technique(s)
western blot: suitable
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... EGFR(1956)
General description
The EGFR family includes four receptor tyrosine kinases, EGF R (ErbB1), ErbB2 (neu), ErbB3, and ErbB4. EGF R is present on many cell types of epithelial and mesenchymal lineages.
The gene EGFR (Epidermal Growth Factor Receptor) is mapped to human chromosome 7p11.2.
Immunogen
synthetic phosphopeptide derived from the region of EGFR that contains tyrosine 1068.
Application
Anti-phospho-EGFR [pTyr1068] antibody may be used at a working dilution of 1:1000 for immunoblotting using NIH3T3 cells expressing human EGF R, stimulated with EGF. The antibody has been in detection of EGF R [pTyr1068] in human lymphocytes.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Biochem/physiol Actions
The members of epidermal growth factor receptor (EGF R) or the ErbB receptor family have been identified as useful biomarkers and targets for cancer therapy. EGF R binds EGF and induces tyrosine phosphorylation leading to proliferation of cells. EGF R is capable of binding transforming growth factor-a and heparin-binding EGF in addition to EGF. There are numerous effector molecule activated by EGF R that result in a variety of biological processes such as morphogenesis, cell motility, apoptosis, differentiation and organ repair and maintenance. Deregulation of EGF R signaling is implicated in progression of a wide variety of tumors, invasion and metastasis. Phosphorylation of Tyr1068 occurs by autophosphorylation of EGF R and is required for the binding of Grb2 and activation of ERK1/2 pathway Anti-phospho-EGFR [pTyr1068] specifically recognizes human and rat EGFR phosphorylated at tyrosine 1068.
Physical form
Solution in Dulbecco′s phosphate buffered saline, with 50% glycerol, 1 mg/ml BSA and 0.05% sodium azide.
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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Certificates of Analysis (COA)
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Adrian P Rybak et al.
PloS one, 8(4), e61716-e61716 (2013-04-27)
Prostate cancer stem-like cells (PCSCs) are being intensely investigated largely owing to their contributions towards prostate tumorigenesis, however, our understanding of PCSC biology, including their critical pathways, remains incompletely understood. While epidermal growth factor (EGF) is widely used in maintaining
Gergely Keszler et al.
Archives of biochemistry and biophysics, 436(1), 69-77 (2005-03-09)
The inborn deficiency of adenosine deaminase is characterised by accumulation of excess amounts of cytotoxic deoxyadenine nucleotides in lymphocytes. Formation of dATP requires phosphorylation of deoxyadenosine by deoxycytidine kinase (dCK), the main nucleoside salvage enzyme in lymphoid cells. Activation of
L Lanzetti et al.
Nature, 408(6810), 374-377 (2000-12-01)
How epidermal growth factor receptor (EGFR) signalling is linked to EGFR trafficking is largely unknown. Signalling and trafficking involve small GTPases of the Rho and Rab families, respectively. But it remains unknown whether the signalling relying on these two classes
Targeting the EGFR signaling pathway in cancer therapy
Seshacharyulu P et al
Expert Opinion on Therapeutic Targets, 16, 15-31 (2010)
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
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