< 0.5% cross-reactivity observed with available related molecules.< 50% cross-species reactivity observed with species tested.
No significant interference observed with available related molecules.
The Quantikine Mouse EGF R Immunoassay is a 4.5 hour solid phase ELISA designed to measure mouse EGF R levels in cell culture supernates, serum, plasma, and urine. It contains NS0-expressed recombinant mouse EGF R and antibodies raised against the recombinant factor. This immunoassay has been shown to quantitate the recombinant mouse EGF R accurately. Results obtained using natural mouse EGF R showed dose-response curves that were parallel to the standard curves obtained using the recombinant kit standards. These results indicate that this kit can be used to determine relative mass values for natural mouse EGF R.
Intra-Assay Precision (Precision within an assay) Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision
Inter-Assay Precision (Precision between assays) Three samples of known concentration were tested in twenty separate assays to assess inter-assay precision. Assays were performed by at least three technicians using two lots of components
The recovery of mouse EGF R spiked to three levels throughout the range of the assay in various matrices was evaluated.
Average % Recovery
Cell Culture Media (n=4)
To assess the linearity of the assay, samples containing and/or spiked with high concentrations of mouse EGF R were serially diluted with Calibrator Diluent to produce samples with values within the dynamic range of the assay.
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
The EGF R subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER-1, ErbB1, or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoproteins with an extracellular ligand binding domain containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites. The human EGF R cDNA encodes a 1210 amino acid (aa) precursor with a 24 aa signal peptide, a 621 aa extracellular domain (ECD), a 23 aa transmembrane segment, and a 542 aa cytoplasmic domain. Soluble receptors consisting of the extracellular ligand binding domain are generated by alternate splicing in human and mouse. Within the ECD, human EGF R shares 88% aa sequence identity with mouse and rat EGF R. It shares 43% - 44% aa sequence identity with the ECD of human ErbB2, ErbB3, and ErbB4. EGF R binds a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, and epigen. Ligand binding induces EGF R homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, heterodimerization tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis. EGF R is overexpressed in a wide variety of tumors and is the target of several anti-cancer drugs.
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