Anti-ΔEGFR, Recombinant [DH8.3]
Invented at Cancer Research UK London Research Institute: Lincoln's Inn Fields
- Datasheet
- References (3)
- Inventor Info
Info
| Catalogue Number | 153269 |
| Applications | ELISA FACS IHC IP WB |
| Antigen/Gene or Protein Targets | Epidermal growth factor. Truncated EGF receptor (RGFR typeIII/EGFRvIII/deltaEGFR). Recognises an EGFR with truncated extracellular domain, present on human tumours. |
| Synonyms | Avian erythroblastic leukemia viral (v erb b) oncogene homolog, Cell growth inhibiting protein 40, 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 |
| Reactivity | Human |
| Relevance |
Recombinant monoclonal antibody directed against ΔEGFR, a mutated form of EGFR, typically found in brain tumours, with use in radiolabelled tumour imaging and potentially therapeutic targeting against ΔEGFR 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. 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. This ΔEGFR mutation is found in particularly high concentrations within glioblastoma. Recombinant anti-ΔEGFR [DH8.3] is raised to a synthetic peptide that recognises the junctional region of the ΔEGFR receptor, raised from the anti-ΔEGFR monoclonal antibody. 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. |
| Host | Mouse |
| Immunogen | Synthetic peptide corresponding to the junctional region of the truncated receptor LEEKKGNYVVTDHC,conjugated to keyhole limpet haemcyanin. |
| Subclass | IgG1 |
| Formulation | PBS |
| Concentration | 1mgml-1 |
| Research Area | Cancer, Cell Signaling & Signal Transduction |
| Immunogen UniProt ID | P00533 |
| Notes |
Production Details Purified using multi-step affinity chromatography with protein A. Storage Conditions Store at -20 degrees frozen. Avoid repeated freeze/thaw cycles. 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. Recombinant monoclonal antibody produced from the original monoclonal cell line. Manufactured using Absolute Antibody’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma. Five different variant available: - Anti-deltaEGFR [DH8.3], Mouse IgG1, Kappa - Anti-deltaEGFR [DH8.3], Rabbit IgG, Kappa - Anti-deltaEGFR [DH8.3], Human IgG4-S228P, Kappa - Anti-deltaEGFR [DH8.3], Human IgG1, Kappa - Anti-deltaEGFR [DH8.3], Human IgG1, Kappa, engineered Fc domain containing key point mutations that abrogate binding to Fc gamma receptors Concentration 1mg/ml as standard |
References: 3 entries
Original hybridoma first published in: Hills et al. 1995. Int J Cancer. 63(4):537-43. PMID: 7591264.
Genßler et al. 2016. Oncoimmunology. 5(4):e1119354. PMID: 27141401.
Feng et al. 2014. J Clin Invest. 124(9):3741-56. PMID: 25061874.
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References: 3 entries
Original hybridoma first published in: Hills et al. 1995. Int J Cancer. 63(4):537-43. PMID: 7591264.
Genßler et al. 2016. Oncoimmunology. 5(4):e1119354. PMID: 27141401.
Feng et al. 2014. J Clin Invest. 124(9):3741-56. PMID: 25061874.
Add a reference
