Recombinant Human EGFR Protein

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

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).

We have publications tested in 1 confirmed species: Human.

We have publications tested in 5 applications: Affinity Purification, Binding Assay, Bioassay, ELISA (Standard), Surface Plasmon Resonance.

Showing Publications 1 - 5 of 5.

Publications using 1095-ER	Applications	Species
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?- A Platform To Enhance Quantitative Single Molecule Localization Microscopy J. Am. Chem. Soc., 2018-09-26;0(0):. 2018-09-26 [PMID: 30256630] (Surface Plasmon Resonance, Human)	Surface Plasmon Resonance	Human
Jarantow S, Bushey B, Pardinas J, Boakye K, Lacy E, Sanders R, Sepulveda M, Moores S, Chiu M Impact of Cell-surface Antigen Expression on Target Engagement and Function of an Epidermal Growth Factor Receptor x c-MET Bispecific Antibody. J Biol Chem, 2015-08-10;290(41):24689-704. 2015-08-10 [PMID: 26260789] (Surface Plasmon Resonance)	Surface Plasmon Resonance
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 Screening and discovery of nitro-benzoxadiazole compounds activating epidermal growth factor receptor (EGFR) in cancer cells. Sci Rep, 2014-02-05;4(0):3977. 2014-02-05 [PMID: 24496106] (Bioassay, Human)	Bioassay	Human
Li N, Nguyen HH, Byrom M, Ellington AD Inhibition of Cell Proliferation by an Anti-EGFR Aptamer. PLoS ONE, 2011-06-08;6(6):e20299. 2011-06-08 [PMID: 21687663] (Affinity Purification, Binding Assay, Human)	Affinity Purification, Binding Assay	Human
Gonzalez RM, Seurynck-Servoss SL, Crowley SA Development and validation of sandwich ELISA microarrays with minimal assay interference. J. Proteome Res., 2008-04-19;7(6):2406-14. 2008-04-19 [PMID: 18422355] (ELISA (Standard))	ELISA (Standard)

Array 1095-ER

• EGFR Antibodies
• EGFR Antibody Pair
• EGFR Lysate
• EGFR Proteins
• EGFR ELISAs
• EGFR Proteins and Enzymes