biological source
rabbit
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
chicken, human, mouse, rat
technique(s)
western blot: 1:1,000 using A431 cells +/- EGF
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
phosphorylation (pTyr1173)
Quality Level
Gene Information
human ... EGFR(1956)
mouse ... Egfr(13649)
General description
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 required for the binding of protein tyrosine phosphatase, SHP-1, which results in dephosphorylation of EFG R
Anti-phospho-EGFR [pTyr1173] specifically recognizes human EGFR phosphorylated at tyrosine 1173. Cross reactivity may be observed with mouse and rat.
Anti-phospho-EGFR [pTyr1173] specifically recognizes human EGFR phosphorylated at tyrosine 1173. Cross reactivity may be observed with mouse and rat.
Immunogen
synthetic phosphopeptide derived from the region of EGFR that contains tyrosine 1173.
Application
Anti-phospho-EGFR [pTyr1173] antibody may be used at a working dilution of 1:1000 for immunoblotting using A431 cells.
Physical form
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) 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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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
新产品
此项目有
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
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
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
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
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.
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