Recombinant Human EGFR Protein Summary
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|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.|
|Reconstitution||Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER2), ErbB3 (HER3), and ErbB4 (HER4). All family members are type I transmembrane glycoproteins that have an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 alpha in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis (1-3).
- Daly, R.J. (1999) Growth Factors, 16:255.
- Schlessinger, J. (2000) Cell. 103:211.
- Maihle, N.J. et al. (2002) Cancer Treat. Res. 107:247.
Citations for Recombinant Human EGFR Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 5
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A Platform To Enhance Quantitative Single Molecule Localization Microscopy
Authors: O Golfetto, DL Wakefield, EE Cacao, KN Avery, V Kenyon, R Jorand, SJ Tobin, S Biswas, J Gutierrez, R Clinton, Y Ma, DA Horne, JC Williams, T Jovanovi?-
J. Am. Chem. Soc., 2018;0(0):.
Sample Types: Antibody
Applications: Surface Plasmon Resonance
Impact of Cell-surface Antigen Expression on Target Engagement and Function of an Epidermal Growth Factor Receptor x c-MET Bispecific Antibody.
Authors: Jarantow S, Bushey B, Pardinas J, Boakye K, Lacy E, Sanders R, Sepulveda M, Moores S, Chiu M
J Biol Chem, 2015;290(41):24689-704.
Sample Types: Protein
Applications: Surface Plasmon Resonance
Screening and discovery of nitro-benzoxadiazole compounds activating epidermal growth factor receptor (EGFR) in cancer cells.
Authors: Sakanyan V, Angelini M, Le Bechec M, Lecocq M, Benaiteau F, Rousseau B, Gyulkhandanyan A, Gyulkhandanyan L, Loge C, Reiter E, Roussakis C, Fleury F
Sci Rep, 2014;4(0):3977.
Sample Types: Recombinant Protein
Inhibition of Cell Proliferation by an Anti-EGFR Aptamer.
Authors: Li N, Nguyen HH, Byrom M, Ellington AD
PLoS ONE, 2011;6(6):e20299.
Sample Types: RNA
Applications: Affinity Purification
Development and validation of sandwich ELISA microarrays with minimal assay interference.
Authors: Gonzalez RM, Seurynck-Servoss SL, Crowley SA
J. Proteome Res., 2008;7(6):2406-14.
Sample Types: N/A
Applications: ELISA (Standard)
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