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Recombinant Human EGFR Isoform vIII Fc Avi-tag Protein, CF

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When Human EGFR Isoform vIII antibody (Novus Catalog # BNP-50599) is immobilized at 0.1 μg/mL (100 μL/well), Biotinylated Recombinant Human EGFR Isoform vIII Fc Chimera Avi-tag (AVI10494) binds with an ED50 of 25-150 ...read more
2 μg/lane of Biotinylated Recombinant Human EGFR Isoform vIII Fc Avi-tag Protein (AVI10494) 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
Format
Carrier-Free

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Recombinant Human EGFR Isoform vIII Fc Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Human EGFR Isoform vIII antibody (Novus Catalog # 50599) is immobilized at 0.1 µg/mL (100 µL/well), Biotinylated Recombinant Human EGFR Isoform vIII Fc Chimera Avi-tag (Catalog # AVI10494)binds with an ED50 of 25-150 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human EGFR protein
Human EGFR Isoform vIII
(Leu25-Ser378)
Accession # NP_001333870.1
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Leu25
Structure / Form
Disulfide-linked homodimer, biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
67 kDa.
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
95-115 kDa, under reducing conditions
Publications
Read Publications using
AVI10494 in the following applications:

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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human EGFR Isoform vIII Fc Avi-tag 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

Epidermal growth factor receptor (EGFR), also known as HER-1 and ErbB1, is a member of a subfamily of receptor tyrosine kinases comprised of four members: EGFR, ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoproteins with an extracellular domain (ECD) containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites (1, 2). Several soluble isoforms lacking the intracellular domain are generated by alternate splicing (3‑4). EGFRvIII is a tumor‐specific mutation that results from an in‐frame deletion removing 267 amino acids from the ECD and insertion of a glycine residue (5). EGFRvIII has a molecular mass of approximately 145 kDa and has been shown to have weaker activity than full-length EGFR (6). 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 (7‑9). 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 (7-9). EGFR is overexpressed in a wide variety of tumors, with EGFRvIII overexpressed particularly in glioblastoma multiforme (GMB), and is the target of several anti-cancer therapeutics (5,10,11). Our Avi-tag Biotinylated Recombinant Human EGFRvIII features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
  1. Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
  2. Shilo, B.Z. (2005) Development 132:4017.
  3. Guillaudeau, A. et al. (2012) PLoS One. 7:1.
  4. Reiter J.L. et al. (2001) Genomics 71:1.
  5. Gan HK et al. (2013) FEBS J. 280:5350
  6. Batra SK, et al. (1995) Cell Growth Differ 6:1251
  7. Freed, D. M. et al. (2017) Cell. 171:683.
  8. Burgess, A.W. et al. (2003) Mol. Cell 12:541.
  9. Faria, J. A. et al. (2016) BBRC. 478:39.
  10. An Z. et al. (2018) Oncogene. 37:1561.
  11. Lee, C. K. et al. (2017) J. Thoracic Oncology. 12:403.

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Publications for EGFR (AVI10494)(2)

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FAQs for EGFR (AVI10494) (0)

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