Anti-deltaEGFR [DH8.3] mAb

Monoclonal antibody directed against deltaEGFR, also known as EGFRvIII, a mutated form of EGFR, typically found in glioblastomas. This antibody has use within radiolabelled tumour imaging and potentially therapeutic targeting against deltaEGFR tumours.

Contributors

Inventor Institute
Bill Gullick Cancer Research UK, London Research Institute: Lincoln's Inn Fields
Cat. #: 152934
Tool sub type: Primary antibody
Unit size: 100 ug
Cancer types: Brain cancer
Research Fields: Cancer;Cell signaling and signal transduction
Application: ELISA ; FACS ; IHC ; IP ; WB
Target: Epidermal growth factor receptor, truncated EGF receptor (RGFR typeIII/EGFRvIII/deltaEGFR). Recognises an EGFR with truncated extracellular domain, present on human tumours.
Reactivity: Human
Clone: DH8.3
Host: Mouse
Class: Monoclonal
Primary citation: Hills et al. 1995. Int J Cancer. 63(4):537-43. PMID: 7591264.
Alternate name: 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-onc…
Product description: Monoclonal antibody directed against ΔEGFR, 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 ΔEGFR tumours. Background and Research Applications: 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. ΔEGFR 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. Anti-ΔEGFR [DH8.3] is raised to a synthetic peptide that recognises the junctional region of the ΔEGFR receptor. Points of Interest 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.
Conjugation: Unconjugated
Isotype: IgG1 kappa
Immunogen: Synthetic peptide corresponding to the junctional region of the truncated receptor LEEKKGNYVVTDHC,conjugated to keyhole limpet haemcyanin.
Immunogen Uniprot ID: P00533
Myeloma used: NS0
Target background: ΔEGFR is the most common alteration observed in glioblastomas. It has a deletion of exons 2 to 7 in the external domain of wt-EGFR, generating a truncated form of EGFR. This truncated EGFRvIII is constitutively active. In this 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.
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: Dry ice
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

Images

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schematic illustrating the truncation of EGFR resulting in EGFRvIII.

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