Mouse EGFR Quantikine ELISA Kit Summary
Product Summary
Precision
Cell Culture Supernates, Serum, EDTA Plasma, Heparin Plasma
Intra-Assay Precision | Inter-Assay Precision | |||||
---|---|---|---|---|---|---|
Sample | 1 | 2 | 3 | 1 | 2 | 3 |
n | 20 | 20 | 20 | 20 | 20 | 20 |
Mean (ng/mL) | 1.11 | 2.58 | 5.41 | 0.976 | 2.42 | 5.13 |
Standard Deviation | 0.049 | 0.08 | 0.159 | 0.09 | 0.114 | 0.197 |
CV% | 4.4 | 3.1 | 2.9 | 9.2 | 4.7 | 3.8 |
Recovery
The recovery of mouse EGF R spiked to three levels throughout the range of the assay in various matrices was evaluated.
Sample Type | Average % Recovery | Range % |
---|---|---|
Cell Culture Media (n=4) | 103 | 94-107 |
Urine (n=4) | 86 | 79-94 |
Linearity
Scientific Data
Product Datasheets
Preparation and Storage
Background: EGFR
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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