Recombinant Mouse EGFR Fc Chimera Protein, CF

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

Recombinant Mouse EGFR Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Recombinant Mouse EGFR Fc Chimera Protein binds to Recombinant Mouse EGF Protein (Catalog # 2028-EG) with an ED₅₀ of 0.500‑5.00 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse EGFR protein
  

  Mouse EGFR (Leu25-Ser647) Accession # Q9EP98	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q9EP98
• N-terminal Sequence: Leu25
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Egfr
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 95.9 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: 118-130 kDa, 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 with trehalose.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• 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 Mouse 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. They contain an extracellular ligand binding domain containing two cysteine-rich domains and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites (1, 2). The mouse EGFR cDNA encodes a 1210 amino acid (aa) precursor with a 24 aa signal peptide, a 623 aa extracellular domain (ECD), a 23 aa transmembrane segment, and a 540 aa cytoplasmic domain (3). Soluble receptors consisting of the extracellular ligand binding domain are generated by alternate splicing in human and mouse (4-6). Within the ECD, mouse EGFR shares 88% and 93% aa sequence identity with human and rat EGFR, respectively. It shares 44%-48% aa sequence identity with the ECD of mouse 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 (7-11). 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 (12, 13). EGFR is over-expressed in a wide variety of tumors and is the target of several anti-cancer drugs (14).

1. Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
2. Shilo, B.Z. (2005) Development 132:4017.
3. Avivi, A. et al. (1991) Oncogene 6:673.
4. Reiter, J.L. and N.J. Maihle (1996) Nucleic Acids Res. 24:4050.
5. Reiter J.L. et al. (2001) Genomics 71:1.
6. Xu, Y.H. et al. (1984) Nature 309:806.
7. Graus-Porta, D. et al. (1997) EMBO J. 16:1647.
8. Yarden, Y. et al. (1987) Biochemistry 26:1434.
9. Burgess, A.W. et al. (2003) Mol. Cell 12:541.
10. Lemmon, M.A. et al. (1997) EMBO J. 16:281.
11. Cohen, S. et al. (1982) J. Biol. Chem. 257:1523.
12. Sibilia, M. and E.F. Wagner (1995) Science 269:234.
13. Miettinen, P.J. et al. (1995) Nature 376:337.
14. Roskoski Jr. R. (2004) Biochem. Biophys. Res. Commun. 319:1.

Publications for EGFR (1280-ER)(2)

Publications using 1280-ER

• 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)
• 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] (Binding Assay, Human)

Bioinformatics

• Gene Symbol: Egfr
• Uniprot:
  • Q9EP98()