Product Image

Contributor Information

  • Name Bill Gullick
  • Institute Cancer Research UK, London Research Institute: Lincoln's Inn Fields
  • Primary citation Hills et al. 1995. Int J Cancer. 63(4):537-43. PMID: 7591264.

Tool Details

  • Tool name: Anti-deltaEGFR [DH8.3] mAb
  • Alternate names: EGFRvIII, Avian erythroblastic leukemia viral (v erb b) oncogene homolog, Cell growth inhibiting protein 4, Cell proliferation inducing protein 61, EGF R, EGFR, Epidermal growth factor receptor (avian erythroblastic leukemia viral (v erb b) oncogene homolog), Epidermal growth factor receptor (erythroblastic leukemia viral (v erb b) oncogene homolog avian), Epidermal growth factor receptor, erb-b2 receptor tyrosine kinase 1, ERBB, ERBB1, Errp, HER1, mENA, NISBD2, Oncogen ERBB, PIG61, Proto-oncogene c-ErbB-1, Receptor tyrosine protein kinase ErbB 1
  • Clone: DH8.3
  • Tool type: Antibodies
  • Tool sub-type: Primary antibody
  • Class: Monoclonal
  • Conjugate: Unconjugated
  • Reactivity: Human
  • Host: Mouse
  • Cancer type: Glioblastoma
  • Cell signalling pathway: EGFR
  • Application: ELISA ; FACS ; IHC ; IP ; WB
  • Description: Monoclonal antibody directed against deltaEGFR, a mutated form of EGFR, typically found in brain tumours, also known as EGFRvIII. This antibody has use within radiolabelled tumour imaging and potentially therapeutic targeting against deltaEGFR tumours.

    Background and Research Application

    Epidermal growth factor (EGFR) has attracted considerable attention as a target for cancer therapy. Wild-type EGFR is amplified in a number of cancers, and several mutant forms of the EGFR coding gene have been found. deltaEGFR is the most common mutation, with a deletion of exons 2-7 in the external domain of wt-EGFR, generating a truncated form of EGFR. This deltaEGFR mutation is found in particularly high concentrations within glioblastoma. Anti-deltaEGFR [DH8.3] is raised to a synthetic peptide that recognises the junctional region of the delataEGFR receptor. It recognises a genetic rearrangement where exon 1 is spliced to exon 8, resulting in the loss of 801 bp from the mature mRNA. This corresponds to a deletion of 267 amino acids in the receptor's extracellular domain. The structure of the receptor is then unable to bind ligand, yet is constitutively active, enhancing tumorigenesis due to impaired internalisation and degradation.

    Points of interest

    Recombinant anti-ΔEGFR [DH8.3] does not recognise the natural, wild-type form of EGFR receptor, so therefore does not cross react with the full-length receptor. It only binds cells expressing the mutant receptor. This antibody can be used in tumour imaging, with radiolabelled antibody DH8.3. This antibody has successfully targeted tumours expressing DH8.3 antigen in nude mice. This antibody recognises ΔEGFR in both denatured and native states.
  • Immunogen: Synthetic peptide corresponding to the junctional region of the truncated receptor LEEKKGNYVVTDHC,conjugated to keyhole limpet haemcyanin.
  • Immunogen UniProt ID: P00533
  • Isotype: IgG1 kappa
  • Research area: Cancer; Cell signaling and signal transduction
  • Myeloma used: NS0

  • For Research Use Only

Target Details

  • Target: Epidermal growth factor receptor, truncated EGF receptor (RGFR typeIII/EGFRvIII/deltaEGFR). Recognises an EGFR with truncated extracellular domain, present on human tumours.
  • Target background: Monoclonal antibody directed against deltaEGFR, a mutated form of EGFR, typically found in brain tumours, also known as EGFRvIII. This antibody has use within radiolabelled tumour imaging and potentially therapeutic targeting against deltaEGFR tumours.

    Background and Research Application

    Epidermal growth factor (EGFR) has attracted considerable attention as a target for cancer therapy. Wild-type EGFR is amplified in a number of cancers, and several mutant forms of the EGFR coding gene have been found. deltaEGFR is the most common mutation, with a deletion of exons 2-7 in the external domain of wt-EGFR, generating a truncated form of EGFR. This deltaEGFR mutation is found in particularly high concentrations within glioblastoma. Anti-deltaEGFR [DH8.3] is raised to a synthetic peptide that recognises the junctional region of the delataEGFR receptor. It recognises a genetic rearrangement where exon 1 is spliced to exon 8, resulting in the loss of 801 bp from the mature mRNA. This corresponds to a deletion of 267 amino acids in the receptor's extracellular domain. The structure of the receptor is then unable to bind ligand, yet is constitutively active, enhancing tumorigenesis due to impaired internalisation and degradation.

Application Details

  • Application: ELISA ; FACS ; IHC ; IP ; WB

Handling

  • Format: Liquid
  • Concentration: 1 mg/ml
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: Store at -20°C frozen. Avoid repeated freeze / thaw cycles
  • Shipping conditions: Shipping at 4°C

Documentation

Related Tools

Product Image

Anti-LPS (F. tularensis) [1F7]

#153708
Product Image

Anti-TAL1 [2TL75]

#151660
Product Image

Anti-DNA [m163-72]

#157812

References

  • •  Genßler et al. 2016. Oncoimmunology. 5(4):e1119354. PMID: 27141401.
  • •  Feng et al. 2014. J Clin Invest. 124(9):3741-56. PMID: 25061874.
  • •  Feng et al. 2012. Proc Natl Acad Sci U S A. 109(8):3018-23. PMID: 22323579.
  • •  Lammering et al. 2004. Clin Cancer Res. 10(19):6732-43. PMID: 15475464.
  • •  Nishikawa et al. 2004. Brain Tumor Pathol. 21(2):53-6. PMID: 15700833.
  • •  Jungbluth et al. 2003. Proc Natl Acad Sci U S A. 100(2):639-44. PMID: 12515857.
  • •  Johns et al. 2002. Int J Cancer. 98(3):398-408. PMID: 11920591.
  • •  Hills et al. 1995. Int J Cancer. 63(4):537-43. PMID: 7591264.