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Recombinant Human EGFR Fc Chimera Protein, CF

R&D Systems | Catalog # 344-ER

Analyzed by SEC-MALS
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Key Product Details

  • R&D Systems NS0-derived Recombinant Human EGFR Fc Chimera Protein (344-ER)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

NS0

Accession Number

CAA25240.1

Structure / Form

Disulfide-linked homodimer

Applications

Binding Activity
View all EGFR Proteins and Enzymes »

Product Specifications

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

Purity

>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.

N-terminal Sequence Analysis

Leu25

Predicted Molecular Mass

95.1 kDa (monomer)

SDS-PAGE

125-145 kDa, under reducing conditions.

Activity

Measured by its ability to bind recombinant human EGF in a functional ELISA with an estimated Kd <8 nM.

Reviewed Applications

Read 2 reviews rated 4.5 using 344-ER in the following applications:

Scientific Data Images for Recombinant Human EGFR Fc Chimera Protein, CF

Recombinant Human EGFR Fc Chimera Protein SEC-MALS

Recombinant Human EGFR Fc Chimera (Catalog # 344-ER) has a molecular weight (MW) of 229 kDa as analyzed by SEC-MALS, suggesting that this protein is a homodimer. MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).
Graph showing bioactivity of Human EGFR protein

Bioactivity of Human EGFR

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

Formulation, Preparation, and Storage

344-ER
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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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).

References

  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

Alternate Names

EGF R, ErbB, ErbB1, HER-1

Entrez Gene IDs

1956 (Human); 13649 (Mouse); 24329 (Rat); 102138724 (Cynomolgus Monkey)

Gene Symbol

EGFR

UniProt

CAA25240.1

Additional EGFR Products

Product Documents for Recombinant Human EGFR Fc Chimera Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Human EGFR Fc Chimera Protein, CF

For research use only

Citations for Recombinant Human EGFR Fc Chimera Protein, CF

Customer Reviews for Recombinant Human EGFR Fc Chimera Protein, CF (2)

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2 Customer Ratings
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  • Recombinant Human EGFR Fc Chimera Protein, CF
    Name: VALENCIO SALEMA
    Application: Binding assay/Protein-protein interaction
    Verified Customer | Posted 03/06/2019
    Recombinant Human EGFR Fc Chimera Protein, CF 344-ER
  • Recombinant Human EGFR Fc Chimera Protein, CF
    Name: VALENCIO SALEMA
    Application: Binding assay/Protein-protein interaction
    Verified Customer | Posted 10/22/2018

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