Recombinant Human EGFR Fc Chimera Protein, CF

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Graph showing bioactivity of Human EGFR protein
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Product Details
Citations (14)
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Recombinant Human EGFR Fc Chimera Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Measured by its ability to bind recombinant human EGF in a functional ELISA with an estimated Kd <8 nM.
Mouse myeloma cell line, NS0-derived human EGFR protein
Human EGFR
Accession # CAA25240.1
IEGRMD Human IgG1-Fc
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
95.1 kDa (monomer)
125-145 kDa, under reducing conditions.

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Scientific Data

Bioactivity Graph showing bioactivity of Human EGFR protein View Larger

Recombinant human EGFR Fc chimera (344-ER) binds recombinant human EGF (236-EG) in a functional ELISA. The estimated Kd for this interaction is < 8 nM.

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Background: EGFR

The EGFR subfamily of receptor tyrosine kinases comprises four members: EGFR (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 (1, 2). The human EGFR 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 (3, 4). Soluble receptors consisting of the extracellular ligand binding domain are generated by alternate splicing in human and mouse (5‑7). Within the ECD, human EGFR shares 88% aa sequence identity with mouse and rat EGFR. It shares 43%-44% aa sequence identity with the ECD of human ErbB2, ErbB3, and ErbB4. EGFR binds a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, and epigen (1, 2). Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, heterodimerization tyrosine phosphorylation and cell signaling (8‑12). EGFR can also be recruited to form heterodimers with the ligand‑activated ErbB3 or ErbB4. EGFR signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis (13, 14). EGFR is overexpressed in a wide variety of tumors and is the target of several anti-cancer drugs (15).

  1. Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
  2. Shilo, B.Z. (2005) Development 132:4017.
  3. Lin, C. et al. (1984) Science 224:843.
  4. Ullrich, A. et al. (1984) Nature 309:418.
  5. Reiter, J.L. and N.J. Maihle (1996) Nucleic Acids Res. 24:4050.
  6. Reiter J.L. et al. (2001) Genomics 71:1.
  7. Xu, Y.H. et al. (1984) Nature 309:806.
  8. Graus-Porta, D. et al. (1997) EMBO J. 16:1647.
  9. Yarden, Y. et al. (1987) Biochemistry 26:1434.
  10. Burgess, A.W. et al. (2003) Mol. Cell 12:541.
  11. Lemmon, M.A. et al. (1997) EMBO J. 16:281.
  12. Cohen, S. et al. (1982) J. Biol. Chem. 257:1523.
  13. Sibilia, M. and E.F. Wagner (1995) Science 269:234.
  14. Miettinen, P.J. et al. (1995) Nature 376:337.
  15. Roskoski Jr., R. (2004) Biochem. Biophys. Res. Commun. 319:1.
Long Name
Epidermal Growth Factor Receptor
Entrez Gene IDs
1956 (Human); 13649 (Mouse); 24329 (Rat); 102138724 (Cynomolgus Monkey)
Alternate Names
avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; cell growth inhibiting protein 40; cell proliferation-inducing protein 61; EC 2.7.10; EC; EGF R; EGFR; epidermal growth factor receptor (avian erythroblastic leukemia viral (v-erb-b)oncogene homolog); epidermal growth factor receptor; ErbB; ErbB1; ERBB1PIG61; HER1; HER-1; mENA; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1

Citations for Recombinant Human EGFR Fc Chimera Protein, CF

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.

14 Citations: Showing 1 - 10
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  1. Format chain exchange (FORCE) for high-throughput generation of bispecific antibodies in combinatorial binder-format matrices
    Authors: S Dengl, K Mayer, F Bormann, H Duerr, E Hoffmann, B Nussbaum, M Tischler, M Wagner, A Kuglstatte, L Leibrock, C Buldun, G Georges, U Brinkmann
    Nat Commun, 2020;11(1):4974.
    Species: N/A
    Sample Types: Small Molecule
    Applications: ELISA Capture
  2. Design Strategy to Create Antibody Mimetics Harbouring Immobilised Complementarity Determining Region Peptides for Practical Use
    Authors: T Kadonosono, W Yimchuen, Y Ota, K See, T Furuta, T Shiozawa, M Kitazawa, Y Goto, A Patil, T Kuchimaru, S Kizaka-Kon
    Sci Rep, 2020;10(1):891.
    Species: Human
    Sample Types: Protein
    Applications: Direct ELISA
  3. Antibody-like proteins that capture and neutralize SARS-CoV-2
    Authors: T Kondo, Y Iwatani, K Matsuoka, T Fujino, S Umemoto, Y Yokomaku, K Ishizaki, S Kito, T Sezaki, G Hayashi, H Murakami
    Sci Adv, 2020;0(0):.
    Species: Human
    Sample Types: Antibody
    Applications: Affinity
  4. Cancer immunotherapy with T cells carrying bispecific receptors that mimic antibodies
    Authors: S Ahn, J Li, C Sun, K Gao, K Hirabayash, H Li, B Savoldo, R Liu, G Dotti
    Cancer Immunol Res, 2019;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: CAR-T
  5. The S100A4 Protein Signals through the ErbB4 Receptor to Promote Neuronal Survival
    Authors: S Pankratova, J Klingelhof, O Dmytriyeva, S Owczarek, A Renziehaus, N Syed, AE Porter, DT Dexter, D Kiryushko
    Theranostics, 2018;8(14):3977-3990.
    Species: Human
    Sample Types: Serum
  6. Recombinant phosphatidylserine-binding nanobodies for targeting of extracellular vesicles to tumor cells: a plug-and-play approach
    Authors: SAA Kooijmans, JJJM Gitz-Franc, RM Schiffeler, P Vader
    Nanoscale, 2018;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: ELISA (Capture)
  7. Masked Chimeric Antigen Receptor for Tumor-Specific Activation
    Authors: X Han, PD Bryson, Y Zhao, GE Cinay, S Li, Y Guo, N Siriwon, P Wang
    Mol. Ther, 2017;25(1):274-284.
    Species: Human
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  8. A derivative of platelet-derived growth factor receptor alpha binds to the trimer of human cytomegalovirus and inhibits entry into fibroblasts and endothelial cells
    Authors: C Stegmann, D Hochdorfer, D Lieber, N Subramania, D Stöhr, K Laib Sampa, C Sinzger
    PLoS Pathog., 2017;13(4):e1006273.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Heterobifunctional Dyes: Highly Fluorescent Linkers Based on Cyanine Dyes
    Authors: V Wycisk, K Achazi, O Hirsch, C Kuehne, J Dernedde, R Haag, K Licha
    ChemistryOpen, 2017;6(3):437-446.
    Applications: Bioassay
  10. A Highly Diverse and Functional Na�ve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents
    J. Mol. Biol., 2016;0(0):.
    Species: Human
    Sample Types: Protein
    Applications: Direct ELISA
  11. A Novel Bispecific Antibody Targeting EGFR and cMet that is Effective Against EGFR Inhibitor- Resistant Lung Tumors
    Cancer Res, 2016;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  12. A Highly Diverse and Functional Na�ve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents
    Authors: Sachdev S Sidhu
    J. Mol. Biol., 2016;0(0):.
    Applications: Western Blot
  13. A HER2-specific Modified Fc Fragment (Fcab) Induces Antitumor Effects Through Degradation of HER2 and Apoptosis.
    Authors: Leung K, Batey S, Rowlands R, Isaac S, Jones P, Drewett V, Carvalho J, Gaspar M, Weller S, Medcalf M, Wydro M, Pegram R, Mudde G, Bauer A, Moulder K, Woisetschlager M, Tuna M, Haurum J, Sun H
    Mol Ther, 2015;23(11):1722-33.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  14. Design of an optimized scaffold for affibody molecules.
    Authors: Feldwisch J, Tolmachev V, Lendel C, Herne N, Sjoberg A, Larsson B, Rosik D, Lindqvist E, Fant G, Hoiden-Guthenberg I, Galli J, Jonasson P, Abrahmsen L
    J. Mol. Biol., 2010;398(2):232-47.
    Applications: Dot Blot


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Recombinant Human EGFR Fc Chimera Protein, CF
By VALENCIO SALEMA on 03/06/2019
Application: Binding assay/Protein-protein interaction

Recombinant Human EGFR Fc Chimera Protein, CF
By VALENCIO SALEMA on 10/22/2018
Application: Binding assay/Protein-protein interaction