E1655
Anti-phospho-Epidermal Growth Factor Receptor [pTyr1148] antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
Sinonimo/i:
Anti-phospho-EGFR [pTyr1148]
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About This Item
Coniugato:
unconjugated
application:
WB
Clone:
polyclonal
Reattività contro le specie:
human
citations:
5
tecniche:
western blot: 1:1,000 using human epithelial A431 cells stimulated with EGF or mouse hybridoma NIH3T3 cells expressing human EGFR and stimulated with EGF
Origine biologica
rabbit
Livello qualitativo
Coniugato
unconjugated
Forma dell’anticorpo
affinity isolated antibody
Tipo di anticorpo
primary antibodies
Clone
polyclonal
Stato
buffered aqueous glycerol solution
PM
antigen ~170 kDa
Reattività contro le specie
human
tecniche
western blot: 1:1,000 using human epithelial A431 cells stimulated with EGF or mouse hybridoma NIH3T3 cells expressing human EGFR and stimulated with EGF
N° accesso UniProt
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
Informazioni sul gene
human ... EGFR(1956)
Descrizione generale
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. The EGFR family includes four receptor tyrosine kinases, EGF R (ErbB1), ErbB2 (neu), ErbB3, and ErbB4. EGF R binds EGF and induces tyrosine phosphorylation leading to proliferation of cells. EGF R is present on many cell types of epithelial and mesenchymal lineages. EGF R is capable of binding transforming growth factor-α 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 EGF R at Tyr1148 is by autophosphorylation may be required for the binding of protein tyrosine phosphatase, SHP-1, which results in dephosphorylation of EFG R
Anti-phospho-EGFR [pTyr1148] specifically recognizes human EGFR phosphorylated at tyrosine 1148.
Anti-phospho-EGFR [pTyr1148] specifically recognizes human EGFR phosphorylated at tyrosine 1148.
Immunogeno
synthetic phosphopeptide derived from the region of EGFR that contains tyrosine 1148.
Applicazioni
Anti-phospho-EGFR [pTyr1148] antibody may be used at a working dilution of 1:1000 for immunoblotting using A431 cells stimulated with EGF.
Stato fisico
Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, with 50% glycerol, 1.0 mg/mL BSA (IgG, protease free) as a carrier and 0.05% sodium azide.
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10 - Combustible liquids
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H Keilhack et al.
The Journal of biological chemistry, 273(38), 24839-24846 (1998-09-12)
The protein-tyrosine phosphatase SHP-1 binds to and dephosphorylates the epidermal growth factor receptor (EGFR), and both SH2 domains of SHP-1 are important for this interaction (Tenev, T., Keilhack, H., Tomic, S., Stoyanov, B., Stein-Gerlach, M., Lammers, R., Krivtsov, A. V.
Parthasarathy Seshacharyulu et al.
Expert opinion on therapeutic targets, 16(1), 15-31 (2012-01-14)
Cancer is a devastating disease; however, several therapeutic advances have recently been made, wherein EGFR and its family members have emerged as useful biomarkers and therapeutic targets. EGFR, a transmembrane glycoprotein is a member of the ERBB receptor tyrosine kinase
A Wells
The international journal of biochemistry & cell biology, 31(6), 637-643 (1999-07-15)
The receptor for the epidermal growth factor (EGF) and related ligands (EGFR), the prototypal member of the superfamily of receptors with intrinsic tyrosine kinase activity, is widely expressed on many cell types, including epithelial and mesenchymal lineages. Upon activation by
Rachana Patel et al.
Current pharmaceutical design, 18(19), 2672-2679 (2012-03-07)
Members of epidermal growth factor receptor (EGFR) or ErbB receptor family play a critical role in a wide range of human cancers. In the past decade, there has been a remarkable progress in developing ErbB targeted therapeutics. However, a substantial
Woody Han et al.
Cancer letters, 318(2), 124-134 (2012-01-21)
The epidermal growth factor receptor (EGFR) pathway is one of the most dysregulated molecular pathways in human cancers. Despite its well-established importance in tumor growth, progression and drug-resistant phenotype over the past several decades, targeted therapy designed to circumvent EGFR
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