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Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 μl per 5 ml antibody dilution buffer for each mini-gel. For immunofluorescence microscopy: Use a dilution range of 1:100~1:400. It is recommended that the reagent be titrated for optimal performance for each application.
COA:
A431 cell extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-EFGR antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
Immunofluorescent microscope analysis of Hela cells using anti-EGFR polyclonal antibody (poly6213) (red). α-tubulin (clone 10D8) has been labeled with green and nuclei were stain with DAPI (blue).
The EGFR is a ubiquitously expressed 180 kD membrane tyrosine kinase that dimerizes upon binding EGF, transforming growth factor alpha, or other ligands. Dimerization initiates downstream signaling that elicits extensive phosphorylation of the receptor resulting in mitogenesis and protection against apoptotic stimuli. EGF receptor expression is amplified in many squamous carcinomas and in the bronchi of high-risk smokers. The receptor is internalized and degraded after ligand binding. EGFR extensively interacts with a number of proteins and is also reported to be a cellular receptor for cytomegalovirus. The Poly6213 antibody recognizes the human, mouse, and rat EGFR and has been shown to be useful for Western blotting.
Membrane tyrosine kinase glycoprotein containing 25 disulphide bridges, 4 FU domains; 170-180 kD. Dimerizes upon ligand binding.
Distribution:
Ubiquitously expressed on the plasma membrane, can also be present in the endosome and nucleus
Function:
EGF receptor binding to EGF (or other ligands) activates receptor-intrinsic tyrosine kinase activity and elicits downstream signaling involving GTPases of the Rho family. Receptor activation initiates a potent mitotic signal required for skin development.
Regulation:
Amplified in many squamous tumors, internalized and degraded after ligand binding
Modification:
Extensively phosphorylated as a result of ligand binding. Also phosphorylated by c-Src, Protein kinase C, and Calcium/calmodulin kinase II
Interaction:
Interacts with Grb2, SHP1 and 2, VAV2 and 3, FAK, c-Src, GAB1, NCK1, Shc, human cytomegalovirus and numerous other proteins
Antigen References:
1. Carpenter G. 1984. Cell 37:357. 2. Ullrich A, et al.1984. Nature 309:418. 3. Reynolds FH, Jr, et al. 1981. Nature 292:259. 4. Sibilia M, et al. 2000. Cell 102:211.
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This data display is provided for general comparisons between formats. Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors. If you need assistance with selecting the best format contact our expert technical support team.
Purified anti-EGFR
A431 cell extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-EFGR antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
Immunofluorescent microscope analysis of Hela cells using anti-EGFR polyclonal antibody (poly6213) (red). α-tubulin (clone 10D8) has been labeled with green and nuclei were stain with DAPI (blue).
