324865
PhosphoDetect Anti-EGFR (pTyr⁸⁴⁵) Rabbit pAb
liquid, Calbiochem®
Synonym(s):
Anti-Epidermal Growth Factor Receptor (pTyr⁸⁴⁵)
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.43
biological source
rabbit
Quality Level
antibody product type
primary antibodies
clone
polyclonal
form
liquid
contains
≤0.1% sodium azide as preservative
species reactivity
human
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
isotype
IgG
shipped in
wet ice
storage temp.
−70°C
target post-translational modification
phosphorylation (pTyr845)
Gene Information
human ... EGFR(1956)
General description
Rabbit polyclonal antibody adsorbed against non-phosphopeptide corresponding to the immunogen phosphorylation site and a generic tyrosine phosphorylated peptide, followed by immunoaffinity chromatography. Recognizes the ~185 KDa EGFR protein phosphorylated on Tyr845.
Recognizes the ~170 kDa EGFR protein phosphorylated at Tyr845 in EGF-treated A431 cells. Note: 1 T = 1 test. Sufficient for 10 Western miniblots.
This PhosphoDetect Anti-EGFR (pTyr⁸⁴⁵) Rabbit pAb is validated for use in Immunoblotting for the detection of EGFR (pTyr⁸⁴⁵).
Immunogen
a synthetic phosphopeptide corresponding to amino acids surrounding the Tyr⁸⁴⁵ phosphorylation site of human EGFR
Application
Immunoblotting (1:1000)
Warning
Toxicity: Standard Handling (A)
Physical form
In Dulbecco′s PBS (w/o Mg2+ and Ca2+), 1 mg/ml BSA, 50% glycerol, pH 7.4.
Reconstitution
Following initial thaw, aliquot and freeze (-70°C).
Analysis Note
Positive Control
A431 cells stimulated with EGF
A431 cells stimulated with EGF
Other Notes
Sieg, D.J. et al. 2000. Nat. Cell. Biol.2, 249.
Barbier, A.J. et al. 1999. J. Biol. Chem.274, 14067.
Biscardi, J.S., et al. 1999. J. Biol. Chem.274, 8335.
Hashimoto, A. et al. 1999. J. Biol. Chem.274, 20139
Poppleton, H.M. et al. 1999. Arch. Biochem. Biophys.363, 227.
Barbier, A.J. et al. 1999. J. Biol. Chem.274, 14067.
Biscardi, J.S., et al. 1999. J. Biol. Chem.274, 8335.
Hashimoto, A. et al. 1999. J. Biol. Chem.274, 20139
Poppleton, H.M. et al. 1999. Arch. Biochem. Biophys.363, 227.
The immunogen sequence is 100% conserved in mouse and rat and 93% conserved in chicken EGFR, but cross-reactivity has not been tested. When diluted to 1:1000 there is sufficient antibody to perform 10 miniblots (10 T) at 10 ml per blot. Variables associated with assay conditions will dictate the proper working dilution.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Transmodulation of epidermal growth factor receptor function by cyclic AMP-dependent protein kinase.
A J Barbier et al.
The Journal of biological chemistry, 274(20), 14067-14073 (1999-05-13)
Binding of epidermal growth factor (EGF) to its receptor (EGFR) augments the tyrosine kinase activity of the receptor and autophosphorylation. Exposure of some tissues and cells to EGF also stimulates adenylyl cyclase activity and results in an increase in cyclic
D J Sieg et al.
Nature cell biology, 2(5), 249-256 (2000-05-12)
Here we show that cells lacking focal adhesion kinase (FAK) are refractory to motility signals from platelet-derived and epidermal growth factors (PDGF and EGF respectively), and that stable re-expression of FAK rescues these defects. FAK associates with activated PDGF- and
A Hashimoto et al.
The Journal of biological chemistry, 274(29), 20139-20143 (1999-07-10)
Two adaptor molecules, Grb2 and Shc, have been implicated in the extracellular signal-regulated kinase (ERK) activation by receptor tyrosine kinases such as the epidermal growth factor receptor (EGFR). Here we show that the EGF-mediated ERK activation is abolished by loss
H M Poppleton et al.
Archives of biochemistry and biophysics, 363(2), 227-236 (1999-03-09)
Using peptides epidermal growth factor receptor (EGFR)-13 and EGFR-14, which correspond to residues 645-657 and 679-692, respectively, in the juxtamembrane, cytosolic region of the epidermal growth factor receptor (EGFR) we have investigated the role of specific regions of the receptor
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
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