Recombinant Human EGFR Fc Chimera Protein, CF

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.

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.

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Human EGFR Fc Chimera Protein, CF Summary

• Additional Information: Analyzed by SEC-MALS
• Details of Functionality: Measured by its ability to bind recombinant human EGF in a functional ELISA with an estimated K_d <8 nM.
• Source: Mouse myeloma cell line, NS0-derived human EGFR protein
  

  Human EGFR (Leu25-Ser645) Accession # CAA25240.1	IEGRMD	Human IgG1-Fc (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: CAA25240.1
• N-terminal Sequence: Leu25
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: EGFR
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 95.1 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 125-145 kDa, under reducing conditions.

Packaging, Storage & Formulations

• 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.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human EGFR Fc Chimera Protein, CF

• avian erythroblastic leukemia viral (v-erb-b) oncogene homolog
• cell growth inhibiting protein 40
• cell proliferation-inducing protein 61
• EC 2.7.10
• EC 2.7.10.1
• 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

Background

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.

Show all background references

Publications for EGFR (344-ER)(14)

Publications using 344-ER

• 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 Format chain exchange (FORCE) for high-throughput generation of bispecific antibodies in combinatorial binder-format matrices Nat Commun, 2020-10-02;11(1):4974. 2020-10-02 [PMID: 33009381] (ELISA Capture, N/A)
• T Kondo, Y Iwatani, K Matsuoka, T Fujino, S Umemoto, Y Yokomaku, K Ishizaki, S Kito, T Sezaki, G Hayashi, H Murakami Antibody-like proteins that capture and neutralize SARS-CoV-2 Sci Adv, 2020-10-14;0(0):. 2020-10-14 [PMID: 32948512] (Bioassay, Human)
• T Kadonosono, W Yimchuen, Y Ota, K See, T Furuta, T Shiozawa, M Kitazawa, Y Goto, A Patil, T Kuchimaru, S Kizaka-Kon Design Strategy to Create Antibody Mimetics Harbouring Immobilised Complementarity Determining Region Peptides for Practical Use Sci Rep, 2020-01-21;10(1):891. 2020-01-21 [PMID: 31964960] (Direct ELISA, Human)
• S Ahn, J Li, C Sun, K Gao, K Hirabayash, H Li, B Savoldo, R Liu, G Dotti Cancer immunotherapy with T cells carrying bispecific receptors that mimic antibodies Cancer Immunol Res, 2019-03-06;0(0):. 2019-03-06 [PMID: 30842091] (CAR-T, CAR-T (Bioassay), Human)
• S Pankratova, J Klingelhof, O Dmytriyeva, S Owczarek, A Renziehaus, N Syed, AE Porter, DT Dexter, D Kiryushko The S100A4 Protein Signals through the ErbB4 Receptor to Promote Neuronal Survival Theranostics, 2018-07-01;8(14):3977-3990. 2018-07-01 [PMID: 30083275] (Human)
• SAA Kooijmans, JJJM Gitz-Franc, RM Schiffeler, P Vader Recombinant phosphatidylserine-binding nanobodies for targeting of extracellular vesicles to tumor cells: a plug-and-play approach Nanoscale, 2018-02-01;0(0):. 2018-02-01 [PMID: 29334397] (ELISA (Capture), Human)
• M Yun, DY Kim, JJ Lee, HS Kim, HS Kim, A Pyo, Y Ryu, TY Kim, JH Zheng, SW Yoo, H Hyun, G Oh, J Jeong, M Moon, JH Min, SY Kwon, JY Kim, E Chung, Y Hong, W Lee, HS Kim, JJ Min A High-Affinity Repebody for Molecular Imaging of EGFR-Expressing Malignant Tumors Theranostics, 2017;7(10):2620-2633. 2017 [PMID: 28819451] (ELISA Developmet, N/A)
• V Wycisk, K Achazi, O Hirsch, C Kuehne, J Dernedde, R Haag, K Licha Heterobifunctional Dyes: Highly Fluorescent Linkers Based on Cyanine Dyes ChemistryOpen, 2017-04-13;6(3):437-446. 2017-04-13 [PMID: 28638777] (Bioassay)
• C Stegmann, D Hochdorfer, D Lieber, N Subramania, D Stöhr, K Laib Sampa, C Sinzger A derivative of platelet-derived growth factor receptor alpha binds to the trimer of human cytomegalovirus and inhibits entry into fibroblasts and endothelial cells PLoS Pathog., 2017-04-12;13(4):e1006273. 2017-04-12 [PMID: 28403220] (Bioassay, Human)
• X Han, PD Bryson, Y Zhao, GE Cinay, S Li, Y Guo, N Siriwon, P Wang Masked Chimeric Antigen Receptor for Tumor-Specific Activation Mol. Ther, 2017-01-04;25(1):274-284. 2017-01-04 [PMID: 28129121] (Flow Cytometry, Human)
• Sachdev S Sidhu A Highly Diverse and Functional Na�ve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents J. Mol. Biol., 2016-11-22;0(0):. 2016-11-22 [PMID: 27887869] (Direct ELISA, Western Blot, Human)
• A Novel Bispecific Antibody Targeting EGFR and cMet that is Effective Against EGFR Inhibitor- Resistant Lung Tumors Cancer Res, 2016-05-23;0(0):. 2016-05-23 [PMID: 27216193] (Bioassay, Human)
• 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 A HER2-specific Modified Fc Fragment (Fcab) Induces Antitumor Effects Through Degradation of HER2 and Apoptosis. Mol Ther, 2015-08-03;23(11):1722-33. 2015-08-03 [PMID: 26234505] (Bioassay, Human)
• 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 Design of an optimized scaffold for affibody molecules. J. Mol. Biol., 2010-03-10;398(2):232-47. 2010-03-10 [PMID: 20226194] (Dot Blot)

Bioinformatics

• Gene Symbol: EGFR
• Uniprot:
  • CAA25240.1()