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Recombinant Human EGFR Fc Chimera Alexa Fluor® 488 Protein

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Streptavidin coated beads conjugated to biotinylated Anti-Human EGFR were stained with the indicated concentrations of Recombinant Human EGFR Fc-tag Alexa Fluor® 488 (Catalog # AFG344).
2 μg/lane of Recombinant Human EGFR Fc Chimera Alexa Fluor® 488 Protein (Catalog # AFG344) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

Order Details

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Recombinant Human EGFR Fc Chimera Alexa Fluor® 488 Protein Summary

Details of Functionality
Measured by flow cytometry for its ability to bind anti-human EGFR Monoclonal Antibody conjugated beads. The concentration of Recombinant Human EGFR Fc-tag Alexa Fluor® 488 (Catalog # AFG344) that produces 50% of the binding response is 8.00-120 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human EGFR protein
Human EGFR
(Leu25-Ser645)
Accession # CAA25240.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Leu25
Structure / Form
Disulfide-linked homodimer
Labeled with Alexa Fluor® 488 via amines
Excitation Wavelength: 488 nm
Emission Wavelength: 515-545 nm
Protein/Peptide Type
Recombinant Proteins
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
  • Bioactivity
Theoretical MW
95 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
118-134 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

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

Alternate Names for Recombinant Human EGFR Fc Chimera Alexa Fluor® 488 Protein

  • 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.

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