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c-Myc antibody | 9E10

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F * 0.1 mg loader
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Mouse anti c-myc antibody, clone 9E10 detects the p62c-myc proto-oncogene protein, which is involved in the regulation of the cell cycle and cell growth. C-myc is primarily located to the cell nucleus, but has also been shown to localized to the cytoplasm in several cell lines (Craig et al. 1993). Overexpression of c-myc has been reported in a wide variety of human cancers (Nesbit et al. 1999).

Mouse anti c-myc antibody, clone 9E10 recognizes the sequence EQKLISEEDL and may be used to detect proteins and peptides labelled with molecular tags containing this sequence (Hilpert et al. 2001).

Target Species
Species Cross-Reactivity
Target SpeciesCross Reactivity
Epitope tag
N.B. Antibody reactivity and working conditions may vary between species.
Product Form
Purified IgG conjugated to Fluorescein Isothiocyanate Isomer 1 (FITC) - liquid
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
Buffer Solution
Phosphate buffered saline
Preservative Stabilisers
0.09% sodium azide (NaN3)
1% bovine serum albumin
Synthetic peptide sequence corresponding to the C-terminal region (residues 408-439) of human c-myc conjugated to keyhole limpet hemocyanin.
Approx. Protein Concentrations
IgG concentration 0.1 mg/ml
Fusion Partners
Spleen cells from immunised BALB/c mice were fused with cells of the SP2/0 myeloma cell line.
Max Ex/Em
Fluorophore Excitation Max (nm) Emission Max (nm)
FITC 490 525
For research purposes only
12 months from date of despatch

This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.

Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended. This product is photosensitive and should be protected from light.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
Flow Cytometry 1 Neat
  1. 1 Membrane permeabilization is required for this application. The use of Leucoperm (Product Code BUF09) is recommended for this purpose.
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
Flow Cytometry
Use 10μl of the suggested working dilution to label 1x106 cells in 100μl

How to Use the Spectraviewer

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  • Start by selecting the application you are interested in, with the option to select an instrument from the drop down menu or create a customized instrument
  • Select the fluorophores or fluorescent proteins you want to include in your panel to check compatibility
  • Select the lasers and filters you wish to include
  • Select combined or multi-laser view to visualize the spectra

Description Product Code Applications Pack Size List Price Your Price Quantity
Mouse IgG1 Negative Control:FITC MCA928F F 100 Tests loader
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Description Mouse IgG1 Negative Control:FITC

Description Product Code Applications Pack Size List Price Your Price Quantity
Human Seroblock BUF070A F 50 Test
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Description Human Seroblock
Human Seroblock BUF070B F 200 Test
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Description Human Seroblock

References for c-Myc antibody

  1. Evan, G.I. et al. (1985) Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product.
    Mol Cell Biol. 5 (12): 3610-6.
  2. Spandidos, D.A. et al. (1987) Elevated expression of the myc gene in human benign and malignant breast lesions compared to normal tissue.
    Anticancer Res. 7 (6): 1299-304.
  3. Borodina, I. et al. (2010) Display of wasp venom allergens on the cell surface of Saccharomyces cerevisiae.
    Microb Cell Fact. 9: 74.
  4. Groeger, G. et al. (2007) Co-operative Cdc42 and Rho signalling mediates ephrinB-triggered endothelial cell retraction.
    Biochem J. 404: 23-9.
  5. Hilpert, K. et al. (2001) Anti-c-myc antibody 9E10: epitope key positions and variability characterized using peptide spot synthesis on cellulose.
    Protein Eng. 14: 803-6.
  6. Gohlke, S. et al. (2017) In Vitro and In Vivo Studies on the Structural Organization of Chs3 from Saccharomyces cerevisiae.
    Int J Mol Sci. 18 (4): pii: E702.
  7. Gray, P. et al. (2010) Identification of a novel human MD-2 splice variant that negatively regulates Lipopolysaccharide-induced TLR4 signaling.
    J Immunol. 184: 6359-66.
  8. Duriseti, S. et al. (2010) Antagonistic anti-urokinase plasminogen activator receptor (uPAR) antibodies significantly inhibit uPAR-mediated cellular signaling and migration.
    J Biol Chem. 285: 26878-88.
  9. View The Latest Product References
  10. Tan, P.H. et al. (2005) Creation of tolerogenic human dendritic cells via intracellular CTLA4: a novel strategy with potential in clinical immunosuppression.
    Blood. 106: 2936-43.
  11. Wallace, S.W. et al. (2010) Cdc42 regulates apical junction formation in human bronchial epithelial cells through PAK4 and Par6B.
    Mol Biol Cell. 21: 2996-3006.
  12. Rowshanravan, B. et al. (2014) RasGAP mediates neuronal survival in Drosophila through direct regulation of Rab5-dependent endocytosis.
    J Cell Sci. 127: 2849-61.
  13. Taylor K et al. (2015) Nanocell targeting using engineered bispecific antibodies.
    MAbs. 7 (1): 53-65.
  14. Sharkey, A.M. et al. (2015) Tissue-Specific Education of Decidual NK Cells.
    J Immunol. 195 (7): 3026-32.
  15. Frohnert, C. et al. (2014) Importin 7 and Nup358 promote nuclear import of the protein component of human telomerase.
    PLoS One. 9 (2): e88887.
  16. Hage, N. et al. (2015) Improved expression and purification of the Helicobacter pylori adhesin BabA through the incorporation of a hexa-lysine tag.
    Protein Expr Purif. 106: 25-30.
  17. Mann, J.K. & Park, S. (2015) Epitope-Specific Binder Design by Yeast Surface Display.
    Methods Mol Biol. 1319: 143-54.
  18. Paraskevopoulou, V. et al. (2019) Introduction of a C-terminal hexa-lysine tag increases thermal stability of the LacDiNac binding adhesin (LabA) exodomain from Helicobacter pylori.
    Protein Expr Purif. 163: 105446.
  19. Lim, H.K. et al. (2010) Flow cytometric analysis of genetic FRET detectors containing variable substrate sequences.
    Biotechnol Prog. 26 (6): 1765-71.
  20. Walker, L.M. et al. (2009) Efficient recovery of high-affinity antibodies from a single-chain Fab yeast display library.
    J Mol Biol. 389 (2): 365-75.
  21. Matos, J. et al. (2013) Cell-cycle kinases coordinate the resolution of recombination intermediates with chromosome segregation.
    Cell Rep. 4 (1): 76-86.
  22. Paraskevopoulou, V. et al. (2020) Structural and binding characterization of the LacdiNAc-specific adhesin (LabA; HopD) exodomain from Helicobacter pylori.
    Curr Res Struct Biol. 15 Dec [Epub ahead of print].
  23. Kalusche, S. et al. (2020) Lactobacilli Expressing Broadly Neutralizing Nanobodies against HIV-1 as Potential Vectors for HIV-1 Prophylaxis?
    Vaccines (Basel). 8 (4) Dec 13 [Epub ahead of print].
  24. Hollandsworth, H.M. et al. (2020) Fluorophore-conjugated Helicobacter pylori recombinant membrane protein (HopQ) labels primary colon cancer and metastases in orthotopic mouse models by binding CEA-related cell adhesion molecules.
    Transl Oncol. 13 (12): 100857.
  25. Paraskevopoulou, V. et al. (2021) Structural and binding characterization of the LacdiNAc-specific adhesin (LabA; HopD) exodomain from Helicobacter pylori.
    Curr Res Struct Biol. 3: 19-29.
  26. Low, S. et al. (2020) VHH antibody targeting the chemokine receptor CX3CR1 inhibits progression of atherosclerosis.
    MAbs. 12 (1): 1709322.

Further Reading

  1. Nesbit, C. et al. (1999) MYC oncogenes and human neoplastic disease.
    Oncogene. 18: 3004-16.
  2. Krauß, N. et al. (2008) The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops.
    Proteins. 73: 552-65.

Flow Cytometry


Western Blotting

Entrez Gene
GO Terms
GO:0005515 protein binding
GO:0001658 branching involved in ureteric bud morphogenesis
GO:0003700 sequence-specific DNA binding transcription factor activity
GO:0005654 nucleoplasm
GO:0005730 nucleolus
GO:0006357 regulation of transcription from RNA polymerase II promoter
GO:0006879 cellular iron ion homeostasis
GO:0007050 cell cycle arrest
GO:0008283 cell proliferation
GO:0042493 response to drug
GO:0016563 transcription activator activity
GO:0032204 regulation of telomere maintenance
GO:0070888 E-box binding
GO:0090096 positive regulation of metanephric cap mesenchymal cell proliferation


159421 1605

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