c-Myc antibody | 9E10
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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 (
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 (
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Epitope tag
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG conjugated to Biotin - 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 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.
- For research purposes only
- 12 months from date of despatch
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Frozen|
|Immunohistology - Paraffin|
|Western Blotting 1|
- 19E10 recognizes c-myc under non-reducing conditions
- Flow Cytometry
- Use 10ul of the suggested working dilution to label 1x106 cells in 100ul.
- This product does not require protein digestion pre-treatment of paraffin sections prior to staining This product does not require antigen retrieval using heat treatment prior to staining of paraffin sections.
References for c-Myc antibody
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.
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.
Borodina, I. et al. (2010) Display of wasp venom allergens on the cell surface of Saccharomyces cerevisiae.
Microb Cell Fact. 9: 74.
Groeger, G. et al. (2007) Co-operative Cdc42 and Rho signalling mediates ephrinB-triggered endothelial cell retraction.
Biochem J. 404: 23-9.
Head, B. et al. (2009) Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells.
J Cell Biol. 187: 959-66.
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.
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.
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.
View The Latest Product References
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.
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.
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.
Rowshanravan, B. et al. (2014) RasGAP mediates neuronal survival in Drosophila through direct regulation of Rab5-dependent endocytosis.
J Cell Sci. 127: 2849-61.
Taylor K et al. (2015) Nanocell targeting using engineered bispecific antibodies.
MAbs. 7 (1): 53-65.
Elders, R.C. et al. (2014) Recombinant canine IgE Fc and an IgE Fc-TRAIL fusion protein bind to neoplastic canine mast cells.
Vet Immunol Immunopathol. 159 (1-2): 29-40.
Sharkey, A.M. et al. (2015) Tissue-Specific Education of Decidual NK Cells.
J Immunol. 195 (7): 3026-32.
McGough, I.J. et al. (2014) Identification of molecular heterogeneity in SNX27-retromer-mediated endosome-to-plasma-membrane recycling.
J Cell Sci. 127 (Pt 22): 4940-53.
Frohnert, C. et al. (2014) Importin 7 and Nup358 promote nuclear import of the protein component of human telomerase.
PLoS One. 9 (2): e88887.
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.
Mann, J.K. & Park, S. (2015) Epitope-Specific Binder Design by Yeast Surface Display.
Methods Mol Biol. 1319: 143-54.
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.
Lim, H.K. et al. (2010) Flow cytometric analysis of genetic FRET detectors containing variable substrate sequences.
Biotechnol Prog. 26 (6): 1765-71.
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.
Matos, J. et al. (2013) Cell-cycle kinases coordinate the resolution of recombination intermediates with chromosome segregation.
Cell Rep. 4 (1): 76-86.
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].
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].
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.
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.
- 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
- View More GO Terms
- 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
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