Anti-Human cMyc (Clone 9E10) (C590-GRP)

c-Myc is an essential transcription factor that belongs to the superfamily of basic helix-loop- helix DNA-binding proteins that function in normal embryogenesis, acquisition and maintenance of stem cell properties, metabolism, cellular division, and cell death1, 2. c-Myc is also a proto-oncogene, originally identified in Burkitt lymphoma1. Its dysregulation, by mutation or epigenetic modification, has been observed in over 50% of human cancers3. c-Myc regulates various cancer cellular functions, including cell cycle, survival, proliferation, and metabolic reprogramming1, and is associated with tumor aggression and chemoresistance3. c-Myc has been suggested as a target for cancer immunotherapy 2and various methods of inhibition have been studied1, 2, 3. 9E10 was generated by immunizing a BALB/c mouse with a synthetic peptide corresponding to residues 408-432 of human c-Myc conjugated to keyhole limpet hemocyanin via the cysteine residues4. Splenocytes were fused with SP2 myeloma cells. 9E10 failed to immunoprecipitate protein from Colo 320 HSR cell extracts during screening but did detect c-Myc in Western blotting. The 9E10 epitope has become a well-known affinity tag used in recombinant protein expression, i.e., the myc-tag5. The target epitope is the C terminal EQKLISEEDL peptide with the core sequence being LISE5and the crystal structure and binding mode have been solved6. 9E10 detection has highly variable epitope recognition that is dependent on neighboring sequence context7. Additionally, cross-reactivity of 9E10 has been observed in murine cell lines in a fluorescence assay and by Western blotting8.